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Ode (poem)
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Ode is a poem written by the English poet Arthur O'Shaughnessy and first published in 1873.[1] It is often referred to by its first line We are the music makers.
Wikisource has original text related to this article:
Ode (O'Shaughnessy)
The Ode is the first poem in O'Shaughnessy's collection Music and Moonlight (1874). It has nine stanzas, although it is commonly believed to be only three stanzas long. The opening stanza is:
We are the music makers,
And we are the dreamers of dreams,
Wandering by lone sea-breakers,
And sitting by desolate streams;—
World-losers and world-forsakers,
On whom the pale moon gleams:
Yet we are the movers and shakers
Of the world for ever, it seems.
The phrase "movers and shakers" (now almost universally misunderstood as a reference to powerful and worldly individuals and groups) originates here.
The poem has been set to music, or alluded to, many times: Sir Edward Elgar set the ode to music in 1912 in his work entitled The Music Makers, Op 69. The work was dedicated to Elgar's old friend Nicholas Kilburn and the first performance took place at the Birmingham Triennial Music Festival in 1912. Performances available include: The Music Makers, with Sir Adrian Boult conducting the London Philharmonic Orchestra in 1975 (reissued 1999), paired with Elgar's Dream of Gerontius; and the 2006 album Sea Pictures paired with The Music Makers, Simon Wright conducting the Bournemouth Symphony Orchestra. Zoltán Kodály (1882–1967) also set the ode to music in his work Music Makers, dedicated to Merton College, Oxford on the occasion of its 700th anniversary in 1964.
The Hungarian composer Zoltán Kodály also made a setting for and dedicated to Merton College, Oxford on the occasion of its 700th anniversary in 1964.
Cultural references and parodies[edit]
In the feature film Willy Wonka & the Chocolate Factory, after Willy Wonka (Gene Wilder) states that "The snozzberries taste like snozzberries!", Veruca Salt responds in an arrogant tone, "Snozzberries? Who ever heard of a snozzberry?" Willy Wonka grabs her cheeks, pulls her face towards him and gently replies, "We are the music makers, and we are the dreamers of dreams."
The line is played during the 89th Academy Awards In Memoriam section, when Gene Wilder is honored.
A sample of Willy Wonka's line appears at the beginning of Bassnectar's album Motions of Mutation.
Wonka's line is played at the beginning of Bastille's cover of "Dreams" by Fleetwood Mac.
The track "Nephatiti" from 808 State's album Ex:el uses a sample of Willy Wonka saying "We are the music makers, and we are the dreamers of dreams."
The introduction of the song "Nothing Less (Ft. Slug)" by the rap group Living Legends begins with the sample of Willy Wonka.
The track "Tighten Up" from The Specktator's album "About That Life" features an introduction of a sample of Willy Wonka saying "We are the music makers, and we are the dreamers of dreams." The same track on Spotify does not feature the same introduction.
The Aphex Twin track "We Are the Music Makers" from Selected Ambient Works 85-92 begins with a sample of Willy Wonka. It is repeated a number of times throughout the track.
Echolyn's 1992 song "A Little Nonsense" contains a sample of Wonka saying the phrase. The song's title also references another quote which Wonka sings, "A little nonsense now and then / Is relished by the wisest men."
The Gathering's instrumental song "Diamond Box" begins with a sample of Wonka's line.
The podcast The Music Makers begins with a sample of Wonka saying the phrase.
Scarling. has a song called "We Are the Music Makers." The line is said in the beginning of the chorus.
The first stanza is quoted in the animated TV show American Dad! on Season 5, Episode 6.
DJ Zinc's track "Music Makers" repeats this phrase throughout the song.
Joy Electric's 1996 album We Are the Music Makers is a reference to the first line.
The track "Movers And Shakers" by Eden Burning begins with a setting of the first stanza of "Ode."
The track "Music Makers" by ILS the track starts off with "We are the music makers, and we are the dreamers of dreams."
"Ode" is quoted at the end of the movie Last Summer in the Hamptons (1995).
The initial verse is used at the start of the Raymond E. Feist novel Rage of a Demon King.
In the Hollywood party scene in Stephen Sondheim's musical Merrily We Roll Along, the character Mary sardonically surveys the other guests and comments "These are the movers / These are the shapers / These are the people / That fill the papers."
The poem is used in the introduction of Elizabeth Haydon's book The Assassin King.
The opening line has been incorporated into the name of the New York band We Are the Music Makers, and the Singaporean Orchestra of the Music Makers.
The line “We are the music makers, we are the dreamers of dreams” is also quoted multiple times in the song “Imagineer” by Lange
The line “We are the music makers, we are the dreamers of dreams” was quoted in "Lonely Soul," a Chillout track by the musician Direct.
The line “We are the music makers, we are the dreamers of dreams” is quoted multiple times in the song “Dreamers of Dreams” by Orkidea
The line “We are the music makers, we are the dreamers of dreams” is quoted in the song “From Your Mind Into My Heart” by A Sol Mechanic
The line “We are the music makers, we are the dreamers of dreams” sentence was also used on track "East 98th Street" at Interstate Highway album Man with No Name (musician).
The line "We are the music makers, we are the dreamers of dreams" is quoted in the beginning of HugLife's trap remix of The Weeknd 's "Wicked Games"
The line “We are the music makers, we are the dreamers of dreams” is sampled on the track "Dreamers & Dreams" by Arctic Moon and Bryan Kearney
The line “We are the music makers, we are the dreamers of dreams” is used in the opening part of the song "Ode” by Sylence (Hardstyle Artist).
"Music Makers & Dreamers of Dreams" is a track off the album "As Above, So Below" by "Windmills".
The Seo Linn song "Music Makers", commissioned by RTÉ for the centenary of the 1916 Easter Rising, is in Irish but uses much of the first stanza of "Ode" as its chorus in English.
Three stanzas of the poem are referenced in "Black", a House track by Fabian Reichelt and Raycoux Jr. on the album Circle
South African band, Gimp, performed a rock anthem of the poem in 2005 at Woodstock South Africa
The phrase "We are the dreamers of dreams" is quoted in Episode 7 of the 9th Season of The Big Bang Theory.
The line "We are the music makers and We are the dreamers of dreams" is used in the Leander High School's Marching Band 2017 production "Internal Landscapes".
References[edit]
Jump up ^ O'Shaughnessy, Arthur (4 October 1873). "An Ode". Appleton's Journal. New York, NY: D. Appleton & Company. Retrieved 15 April 2014.
External links[edit]
Full Text of Poem
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Ribosome
From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Cell biology
The animal cell
Components of a typical animal cell:
Nucleolus
Nucleus
Ribosome (little dots)
Vesicle
Rough endoplasmic reticulum
Golgi apparatus (or "Golgi body")
Cytoskeleton
Smooth endoplasmic reticulum
Mitochondrion
Vacuole
Cytosol (fluid that contains organelles, comprising the cytoplasm)
Lysosome
Centrosome
Cell membrane
Figure 1: Ribosomes assemble polymeric protein molecules whose sequence is controlled by the sequence of messenger RNA molecules. This is required by all living cells and associated viruses.
The ribosome (/ˈraɪbəˌsoʊm, -boʊ-/[1]) is a complex molecular machine, found within all living cells, that serves as the site of biological protein synthesis (translation). Ribosomes link amino acids together in the order specified by messenger RNA (mRNA) molecules. Ribosomes consist of two major components: the small ribosomal subunits, which read the RNA, and the large subunits, which join amino acids to form a polypeptide chain. Each subunit comprises one or more ribosomal RNA (rRNA) molecules and a variety of ribosomal proteins (r-protein or rProtein[2][3][4]). The ribosomes and associated molecules are also known as the translational apparatus.
Contents
1 Overview
2 Discovery
3 Structure
3.1 High-resolution structure
4 Function
4.1 Translation
4.2 Addition of translation-independent amino acids
5 Ribosome locations
5.1 Free ribosomes
5.2 Membrane-bound ribosomes
6 Biogenesis
7 Origin
8 Specialized ribosomes
9 See also
10 References
11 External links
Overview[edit]
The sequence of DNA, which encodes the sequence of the amino acids in a protein, is copied into a messenger RNA chain. It may be copied many times into RNA chains. Ribosomes can bind to a messenger RNA chain and use its sequence for determining the correct sequence of amino acids for generating a given protein. Amino acids are selected, collected, and carried to the ribosome by transfer RNA (tRNA) molecules, which enter one part of the ribosome and bind to the messenger RNA chain. It is during this binding that the correct translation of nucleic acid sequence to amino acid sequence occurs. For each coding triplet in the messenger RNA there is a distinct transfer RNA that matches and which carries the correct amino acid for that coding triplet. The attached amino acids are then linked together by another part of the ribosome. Once the protein is produced, it can then fold to produce a specific functional three-dimensional structure although during synthesis some proteins start folding into their correct form.
A ribosome is made from complexes of RNAs and proteins and is therefore a ribonucleoprotein. Each ribosome is divided into two subunits:
a smaller subunit which binds to a larger subunit and the mRNA pattern, and
a larger subunit which binds to the tRNA, the amino acids, and the smaller subunit.
When a ribosome finishes reading an mRNA molecule, these two subunits split apart. Ribosomes are ribozymes, because the catalytic peptidyl transferase activity that links amino acids together is performed by the ribosomal RNA. Ribosomes are often associated with the intracellular membranes that make up the rough endoplasmic reticulum.
Ribosomes from bacteria, archaea and eukaryotes in the three-domain system, resemble each other to a remarkable degree, evidence of a common origin. They differ in their size, sequence, structure, and the ratio of protein to RNA. The differences in structure allow some antibiotics to kill bacteria by inhibiting their ribosomes, while leaving human ribosomes unaffected. In bacteria and archaea, more than one ribosome may move along a single mRNA chain at one time, each "reading" its sequence and producing a corresponding protein molecule.
The mitochondrial ribosomes of eukaryotic cells, are produced from mitochondrial genes, and functionally resemble many features of those in bacteria, reflecting the likely evolutionary origin of mitochondria.[5][6]
Discovery[edit]
Ribosomes were first observed in the mid-1955s by Romanian-American cell biologist George Emil Palade, using an electron microscope, as dense particles or granules.[7] The term "ribosome" was proposed by scientist Richard B. Roberts in the end of 1950s:
During the course of the symposium a semantic difficulty became apparent. To some of the participants, "microsomes" mean the ribonucleoprotein particles of the microsome fraction contaminated by other protein and lipid material; to others, the microsomes consist of protein and lipid contaminated by particles. The phrase "microsomal particles" does not seem adequate, and "ribonucleoprotein particles of the microsome fraction" is much too awkward. During the meeting, the word "ribosome" was suggested, which has a very satisfactory name and a pleasant sound. The present confusion would be eliminated if "ribosome" were adopted to designate ribonucleoprotein particles in sizes ranging from 35 to 100S.
—  Albert, Microsomal Particles and Protein Synthesis[8]
Albert Claude, Christian de Duve, and George Emil Palade were jointly awarded the Nobel Prize in Physiology or Medicine, in 1974, for the discovery of the ribosome.[9] The Nobel Prize in Chemistry 2009 was awarded to Venkatraman Ramakrishnan, Thomas A. Steitz and Ada E. Yonath for determining the detailed structure and mechanism of the ribosome.[10]
Structure[edit]
Figure 2: Large (red) and small (blue) subunit fit together.
The ribosome is a highly complex cellular machine. It is largely made up of specialized RNA known as ribosomal RNA (rRNA) as well as dozens of distinct proteins (the exact number varies slightly between species). The ribosomal proteins and rRNAs are arranged into two distinct ribosomal pieces of different size, known generally as the large and small subunit of the ribosome. Ribosomes consist of two subunits that fit together (Figure 2) and work as one to translate the mRNA into a polypeptide chain during protein synthesis (Figure 1). Because they are formed from two subunits of non-equal size, they are slightly longer in the axis than in diameter.
Prokaryotic ribosomes are around 20 nm (200 Å) in diameter and are composed of 65% rRNA and 35% ribosomal proteins.[11] Eukaryotic ribosomes are between 25 and 30 nm (250–300 Å) in diameter with an rRNA-to-protein ratio that is close to 1.[12] Crystallographic work [13] has shown that there are no ribosomal proteins close to the reaction site for polypeptide synthesis. This suggests that the protein components of ribosomes do not directly participate in peptide bond formation catalysis, but rather that these proteins act as a scaffold that may enhance the ability of rRNA to synthesize protein (See: Ribozyme).
Figure 3: Atomic structure of the 30S subunit from Thermus thermophilus.[14] Proteins are shown in blue and the single RNA chain in orange.
The ribosomal subunits of prokaryotes and eukaryotes are quite similar.[15]
The unit of measurement used to describe the ribosomal subunits and the rRNA fragments is the Svedberg unit, a measure of the rate of sedimentation in centrifugation rather than size. This accounts for why fragment names do not add up: for example, prokaryotic 70S ribosomes are made of 50S and 30S subunits.
Prokaryotes have 70S ribosomes, each consisting of a small (30S) and a large (50S) subunit. Their small subunit has a 16S RNA subunit (consisting of 1540 nucleotides) bound to 21 proteins. The large subunit is composed of a 5S RNA subunit (120 nucleotides), a 23S RNA subunit (2900 nucleotides) and 31 proteins.[15]
prokaryotic ribosomes (E. coli)[16]
ribosome
subunit
rRNAs
r-proteins
70S 50S 23S (2904 nt) 31
5S (120 nt)
30S 16S (1542 nt) 21
Affinity label for the tRNA binding sites on the E. coli ribosome allowed the identification of A and P site proteins most likely associated with the peptidyltransferase activity; labelled proteins are L27, L14, L15, L16, L2; at least L27 is located at the donor site, as shown by E. Collatz and A.P. Czernilofsky.[17][18] Additional research has demonstrated that the S1 and S21 proteins, in association with the 3′-end of 16S ribosomal RNA, are involved in the initiation of translation.[19]
Eukaryotes have 80S ribosomes, each consisting of a small (40S) and large (60S) subunit. Their 40S subunit has an 18S RNA (1900 nucleotides) and 33 proteins.[20][21] The large subunit is composed of a 5S RNA (120 nucleotides), 28S RNA (4700 nucleotides), a 5.8S RNA (160 nucleotides) subunits and 46 proteins.[15][20][22]
eukaryotic cytosolic ribosomes (R. norvegicus)[23]
ribosome
subunit
rRNAs
r-proteins
80S 60S 28S (4718 nt) 49
5.8S (160 nt)
5S (120 nt)
40S 18S (1874 nt) 33
During 1977, Czernilofsky published research that used affinity labeling to identify tRNA-binding sites on rat liver ribosomes. Several proteins, including L32/33, L36, L21, L23, L28/29 and L13 were implicated as being at or near the peptidyl transferase center.[24]
The ribosomes found in chloroplasts and mitochondria of eukaryotes also consist of large and small subunits bound together with proteins into one 70S particle.[15] These organelles are believed to be descendants of bacteria (see Endosymbiotic theory) and, as such, their ribosomes are similar to those of bacteria.[15]
The various ribosomes share a core structure, which is quite similar despite the large differences in size. Much of the RNA is highly organized into various tertiary structural motifs, for example pseudoknots that exhibit coaxial stacking. The extra RNA in the larger ribosomes is in several long continuous insertions, such that they form loops out of the core structure without disrupting or changing it.[15] All of the catalytic activity of the ribosome is carried out by the RNA; the proteins reside on the surface and seem to stabilize the structure.[15]
The differences between the bacterial and eukaryotic ribosomes are exploited by pharmaceutical chemists to create antibiotics that can destroy a bacterial infection without harming the cells of the infected person. Due to the differences in their structures, the bacterial 70S ribosomes are vulnerable to these antibiotics while the eukaryotic 80S ribosomes are not.[25] Even though mitochondria possess ribosomes similar to the bacterial ones, mitochondria are not affected by these antibiotics because they are surrounded by a double membrane that does not easily admit these antibiotics into the organelle.[26]
High-resolution structure[edit]
Figure 4: Atomic structure of the 50S subunit from Haloarcula marismortui. Proteins are shown in blue and the two RNA chains in orange and yellow.[27] The small patch of green in the center of the subunit is the active site.
The general molecular structure of the ribosome has been known since the early 1970s. In the early 2000s, the structure has been achieved at high resolutions, of the order of a few ångströms.
The first papers giving the structure of the ribosome at atomic resolution were published almost simultaneously in late 2000. The 50S (large prokaryotic) subunit was determined from the archaeon Haloarcula marismortui[27] and the bacterium Deinococcus radiodurans,[28] and the structure of the 30S subunit was determined from Thermus thermophilus.[14] These structural studies were awarded the Nobel Prize in Chemistry in 2009. In May 2001 these coordinates were used to reconstruct the entire T. thermophilus 70S particle at 5.5 Å resolution.[29]
Two papers were published in November 2005 with structures of the Escherichia coli 70S ribosome. The structures of a vacant ribosome were determined at 3.5 Å resolution using X-ray crystallography.[30] Then, two weeks later, a structure based on cryo-electron microscopy was published,[31] which depicts the ribosome at 11–15 Å resolution in the act of passing a newly synthesized protein strand into the protein-conducting channel.
The first atomic structures of the ribosome complexed with tRNA and mRNA molecules were solved by using X-ray crystallography by two groups independently, at 2.8 Å[32] and at 3.7 Å.[33] These structures allow one to see the details of interactions of the Thermus thermophilus ribosome with mRNA and with tRNAs bound at classical ribosomal sites. Interactions of the ribosome with long mRNAs containing Shine-Dalgarno sequences were visualized soon after that at 4.5–5.5 Å resolution.[34]
In 2011, the first complete atomic structure of the eukaryotic 80S ribosome from the yeast Saccharomyces cerevisiae was obtained by crystallography.[20] The model reveals the architecture of eukaryote-specific elements and their interaction with the universally conserved core. At the same time, the complete model of a eukaryotic 40S ribosomal structure in Tetrahymena thermophila was published and described the structure of the 40S subunit, as well as much about the 40S subunit's interaction with eIF1 during translation initiation.[21] Similarly, the eukaryotic 60S subunit structure was also determined from Tetrahymena thermophila in complex with eIF6.[22]
Function[edit]
Ribosomes are minute particles consisting of RNA and associated proteins that function to synthesize proteins. Proteins are needed for many cellular functions such as repairing damage or directing chemical processes. Ribosomes can be found floating within the cytoplasm or attached to the endoplasmic reticulum.
Translation[edit]
Main article: Translation (genetics)
Ribosomes are the workplaces of protein biosynthesis, the process of translating mRNA into protein. The mRNA comprises a series of codons that dictate to the ribosome the sequence of the amino acids needed to make the protein. Using the mRNA as a template, the ribosome traverses each codon (3 nucleotides) of the mRNA, pairing it with the appropriate amino acid provided by an aminoacyl-tRNA. Aminoacyl-tRNA contains a complementary anticodon on one end and the appropriate amino acid on the other. For fast and accurate recognition of the appropriate tRNA, the ribosome utilizes large conformational changes (conformational proofreading) .[35] The small ribosomal subunit, typically bound to an aminoacyl-tRNA containing the amino acid methionine, binds to an AUG codon on the mRNA and recruits the large ribosomal subunit. The ribosome contains three RNA binding sites, designated A, P and E. The A-site binds an aminoacyl-tRNA;[36] the P-site binds a peptidyl-tRNA (a tRNA bound to the peptide being synthesized); and the E-site (exit) binds a free tRNA before it exits the ribosome. Protein synthesis begins at a start codon AUG near the 5' end of the mRNA. mRNA binds to the P site of the ribosome first. The ribosome is able to identify the start codon by use of the Shine-Dalgarno sequence of the mRNA in prokaryotes and Kozak box in eukaryotes.
Although catalysis of the peptide bond involves the C2 hydroxyl of RNA's P-site adenosine in a proton shuttle mechanism, other steps in protein synthesis (such as translocation) are caused by changes in protein conformations. Since their catalytic core is made of RNA, ribosomes are classified as "ribozymes,"[37] and it is thought that they might be remnants of the RNA world.[38]
Figure 5 : Translation of mRNA (1) by a ribosome (2)(shown as small and large subunits) into a polypeptide chain (3). The ribosome begins at the start codon of RNA (AUG) and ends at the stop codon (UAG).
In Figure 5, both ribosomal subunits (small and large) assemble at the start codon (towards the 5' end of the RNA). The ribosome uses RNA that matches the current codon (triplet) on the mRNA to append an amino acid to the polypeptide chain. This is done for each triplet on the RNA, while the ribosome moves towards the 3' end of the mRNA. Usually in bacterial cells, several ribosomes are working parallel on a single RNA, forming what is called a polyribosome or polysome.
Addition of translation-independent amino acids[edit]
Presence of a ribosome quality control protein Rqc2 is associated with mRNA-independent protein elongation.[39][40] This elongation is a result of ribosomal addition (via tRNAs brought by Rqc2) of CAT tails: ribosomes extend the C-terminus of a stalled protein with random, translation-independent sequences of alanines and threonines.[41][42]
Würzburg University and Max Planck Institute researches, the results of which were published in Cell Reports and The EMBO magazines in September 2016, have shown that ribosomes have the role of being "a quality control point". Professor Utz Fischer from the University of Würzburg has been researching the assembly of proteins called "macromolecular machines" in the cell for years. He describes this assembly process as LEGO blocks: "Think of it as LEGO bricks at the molecular level: One brick is attached to the next until the product is finished. If only one defective or wrong brick is used, the entire building may be compromised as a result."[43][44][45]
Ribosome locations[edit]
Ribosomes are classified as being either "free" or "membrane-bound".
Figure 6 : A ribosome translating a protein that is secreted into the endoplasmic reticulum.
Free and membrane-bound ribosomes differ only in their spatial distribution; they are identical in structure. Whether the ribosome exists in a free or membrane-bound state depends on the presence of an ER-targeting signal sequence on the protein being synthesized, so an individual ribosome might be membrane-bound when it is making one protein, but free in the cytosol when it makes another protein.
Ribosomes are sometimes referred to as organelles, but the use of the term organelle is often restricted to describing sub-cellular components that include a phospholipid membrane, which ribosomes, being entirely particulate, do not. For this reason, ribosomes may sometimes be described as "non-membranous organelles".
Free ribosomes[edit]
Free ribosomes can move about anywhere in the cytosol, but are excluded from the cell nucleus and other organelles. Proteins that are formed from free ribosomes are released into the cytosol and used within the cell. Since the cytosol contains high concentrations of glutathione and is, therefore, a reducing environment, proteins containing disulfide bonds, which are formed from oxidized cysteine residues, cannot be produced within it.
Membrane-bound ribosomes[edit]
When a ribosome begins to synthesize proteins that are needed in some organelles, the ribosome making this protein can become "membrane-bound". In eukaryotic cells this happens in a region of the endoplasmic reticulum (ER) called the "rough ER". The newly produced polypeptide chains are inserted directly into the ER by the ribosome undertaking vectorial synthesis and are then transported to their destinations, through the secretory pathway. Bound ribosomes usually produce proteins that are used within the plasma membrane or are expelled from the cell via exocytosis.[46]
Biogenesis[edit]
Main article: Ribosome biogenesis
In bacterial cells, ribosomes are synthesized in the cytoplasm through the transcription of multiple ribosome gene operons. In eukaryotes, the process takes place both in the cell cytoplasm and in the nucleolus, which is a region within the cell nucleus. The assembly process involves the coordinated function of over 200 proteins in the synthesis and processing of the four rRNAs, as well as assembly of those rRNAs with the ribosomal proteins.
Origin[edit]
The ribosome may have first originated in an RNA world, appearing as a self-replicating complex that only later evolved the ability to synthesize proteins when amino acids began to appear.[47] Studies suggest that ancient ribosomes constructed solely of rRNA could have developed the ability to synthesize peptide bonds.[48][49][50] In addition, evidence strongly points to ancient ribosomes as self-replicating complexes, where the rRNA in the ribosomes had informational, structural, and catalytic purposes because it could have coded for tRNAs and proteins needed for ribosomal self-replication.[51] Hypothetical cellular organisms with self-replicating RNA but without DNA are called ribocytes (or ribocells).[52][53]
As amino acids gradually appeared in the RNA world under prebiotic conditions,[54][55] their interactions with catalytic RNA would increase both the range and efficiency of function of catalytic RNA molecules.[47] Thus, the driving force for the evolution of the ribosome from an ancient self-replicating machine into its current form as a translational machine may have been the selective pressure to incorporate proteins into the ribosome’s self-replicating mechanisms, so as to increase its capacity for self-replication.[51]
Specialized ribosomes[edit]
Heterogeneity in ribosome composition has been proposed to be involved in translational control of protein synthesis.[56] Vincent Mauro and Gerald Edelman proposed the ribosome filter hypothesis to explain the regulatory functions of ribosomes. Emerging evidence has shown that specialized ribosomes specific to different cell populations can affect how genes are translated.[57] Some ribosomal proteins exchange from the assembled complex with cytosolic copies [58] suggesting that the structure of the in vivo ribosome can be modified without synthesizing an entire new ribosome.
See also[edit]
Aminoglycosides
Biological machines
Eukaryotic translation
Posttranslational modification
Prokaryotic translation
Protein dynamics
RNA tertiary structure
Translation (genetics)
Wobble base pair
References[edit]
Jump up ^ Jones, Daniel (2003) [1917], Peter Roach, James Hartmann and Jane Setter, eds., English Pronouncing Dictionary, Cambridge: Cambridge University Press, ISBN 3-12-539683-2 CS1 maint: Uses editors parameter (link)
Jump up ^ Salini Konikkat: Dynamic Remodeling Events Drive the Removal of the ITS2 Spacer Sequence During Assembly of 60S Ribosomal Subunits in S. cerevisiae. Archived 2017-08-03 at the Wayback Machine. Carnegie Mellon University Dissertations, February 2016.
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External links[edit]
Wikimedia Commons has media related to Ribosomes.
Lab computer simulates ribosome in motion
Role of the Ribosome, Gwen V. Childs, copied here
Ribosome in Proteopedia - The free, collaborative 3D encyclopedia of proteins & other molecules
Ribosomal proteins families in ExPASy
Molecule of the Month © RCSB Protein Data Bank:
Ribosome
Elongation Factors
Palade
3D electron microscopy structures of ribosomes at the EM Data Bank(EMDB)
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e
Structures of the cell / organelles
Endomembrane system
Cell membrane
Nucleus
Endoplasmic reticulum
Golgi apparatus
Parenthesome
Autophagosome
Vesicles
Exosome
Lysosome
Endosome
Phagosome
Vacuole
Acrosome
Cytoplasmic granules
Melanosome
Microbody
Glyoxysome
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Microtubules
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MTOCs
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Spindle pole body
Myofibril
Endosymbionts
Mitochondrion
Plastids
Chloroplast
Chromoplast
Gerontoplast
Leucoplast
Amyloplast
Elaioplast
Proteinoplast
Tannosome
Other internal
Nucleolus
RNA
Ribosome
Spliceosome
Vault
Cytoplasm
Cytosol
Inclusions
Proteasome
External
Undulipodium
Cilium
Flagellum
Axoneme
Radial spoke
Extracellular matrix
Cell wall
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e
Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)
Proteins
Initiation factor
Bacterial
PIF-1
PIF-2
PIF-3
Archaeal
aIF1
aIF2
aIF5
aIF6
Eukaryotic
eIF1
eIF1
EIF1AX
AY
1B
eIF2
EIF2S1
EIF2S2
EIF2S3
EIF2B1
EIF2B2
EIF2B3
EIF2B4
EIF2B5
EIF-2 kinase
eIF2A
eIF2D
eIF3
EIF3A
B
C
D
E
F
G
H
I
J
K
L
M
eIF4
EIF4A2
A3
B
E1
E2
E3
G1
G2
G3
H
eIF5
EIF5
EIF5A
A2
5B
eIF6
EIF6
Elongation factor
Bacterial
EF-Tu
EF-Ts
EF-G
Archaeal
aEF-1
aEF-2
Eukaryotic
EEF-1
EEF1A1
EEF1A2
EEF1A3
EEF1B1
EEF1B2
EEF1B3
EEF1B4
EEF1D
EEF1E1
EEF1G
EEF2
Release factor
Bacterial
Archaeal
Eukaryotic (ETF1)
Ribosomal Proteins
Cytoplasmic
60S subunit
RPL3
RPL4
RPL5
RPL6
RPL7
RPL7A
RPL8
RPL9
RPL10
RPL10A
RPL10-like
RPL11
RPL12
RPL13
RPL13A
RPL14
RPL15
RPL17
RPL18
RPL18A
RPL19
RPL21
RPL22
RPL23
RPL23A
RPL24
RPL26
RPL27
RPL27A
RPL28
RPL29
RPL30
RPL31
RPL32
RPL34
RPL35
RPL35A
RPL36
RPL36A
RPL37
RPL37A
RPL38
RPL39
RPL40
RPL41
RPLP0
RPLP1
RPLP2
RRP15-like
RSL24D1
40S subunit
RPSA
RPS2
RPS3
RPS3A
RPS4 (RPS4X, RPS4Y1, RPS4Y2)
RPS5
RPS6
RPS7
RPS8
RPS9
RPS10
RPS11
RPS12
RPS13
RPS14
RPS15
RPS15A
RPS16
RPS17
RPS18
RPS19
RPS20
RPS21
RPS23
RPS24
RPS25
RPS26
RPS27
RPS27A
RPS28
RPS29
RPS30
RACK1
Mitochondrial
39S subunit
MRPL1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
28S subunit
MRPS1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
Other concepts
Aminoacyl tRNA synthetase
Reading frame
Start codon
Stop codon
Shine-Dalgarno sequence/Kozak consensus sequence
show
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e
Ribosomal RNA / ribosome subunits
Archaea
Large:
Small:
Bacteria (70S)
Large:
50S
5S
23S
Small:
30S
16S
Eukaryotes (80S)
Cytoplasmic
Large:
60S
5S
5.8S
28S
Small:
40S
18S
Mitochondrial
Large:
MT-RNR2, 16S
Small:
MT-RNR1, 12S
Chloroplast
Large chloroplast subunit
Small chloroplast subunit
This article incorporates public domain material from the NCBI document "Science Primer".
Authority control
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NDL: 00569445
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text:
Furman v. Georgia
From Wikipedia, the free encyclopedia
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Furman v. Georgia
Supreme Court of the United States
Argued January 17, 1972
Decided June 29, 1972
Full case name
William Henry Furman v. State of Georgia
Citations
408 U.S. 238 (more)
92 S. Ct. 2726; 33 L. Ed. 2d 346; 1972 U.S. LEXIS 169
Prior history
Certiorari granted (403 U.S. 952)
Subsequent history
Rehearing denied (409 U.S. 902)
Holding
The arbitrary and inconsistent imposition of the death penalty violates the Eighth and Fourteenth Amendments, and constitutes cruel and unusual punishment.
Court membership
Chief Justice
Warren E. Burger
Associate Justices
William O. Douglas · William J. Brennan, Jr.
Potter Stewart · Byron White
Thurgood Marshall · Harry Blackmun
Lewis F. Powell, Jr. · William Rehnquist
Case opinions
Per curiam.
Concurrence
Douglas
Concurrence
Brennan
Concurrence
Stewart
Concurrence
White
Concurrence
Marshall
Dissent
Burger, joined by Blackmun, Powell, Rehnquist
Dissent
Blackmun
Dissent
Powell, joined by Burger, Blackmun, Rehnquist
Dissent
Rehnquist, joined by Burger, Blackmun, Powell
Laws applied
U.S. Const. amends. VIII, XIV
Wikisource has original text related to this article:
Furman v. Georgia
Furman v. Georgia, 408 U.S. 238 (1972) was a criminal case in which the United States Supreme Court struck down all death penalty schemes in the United States in a 5–4 decision, with each member of the majority writing a separate opinion.[1]:467–8 Following Furman, in order to reinstate the death penalty, states had to at least remove arbitrary and discriminatory effects, to satisfy the Eighth Amendment to the United States Constitution.[1]:468
The decision ruled on the requirement for a degree of consistency in the application of the death penalty. This case led to a de facto moratorium on capital punishment throughout the United States, which came to an end when Gregg v. Georgia was decided in 1976 to allow the death penalty.
The Supreme Court consolidated Jackson v. Georgia and Branch v. Texas with the Furman decision, and thus also invalidated the death penalty for rape (this ruling was confirmed post-Gregg in Coker v. Georgia). The Court had also intended to include the case of Aikens v. California, but between the time Aikens had been heard in oral argument and a decision was to be issued, the Supreme Court of California decided in California v. Anderson that the death penalty violated the state constitution. The Aikens case was dismissed as moot since all death sentences in California were reduced to life imprisonment.
Contents
[hide]
1 Background
2 Decision
3 Dissents
4 Aftermath
5 See also
6 References
7 Further reading
8 External links
Background[edit]
In the Furman v. Georgia case, the resident awoke in the middle of the night to find William Henry Furman committing burglary in his house. At trial, in an unsworn statement allowed under Georgia criminal procedure, Furman said that while trying to escape, he tripped and the weapon he was carrying fired accidentally, killing the victim. This contradicted his prior statement to police that he had turned and blindly fired a shot while fleeing. In either event, because the shooting occurred during the commission of a felony, Furman would have been guilty of murder and eligible for the death penalty under then-extant state law, according to the felony murder rule. Furman was tried for murder and was found guilty based largely on his own statement. Although he was sentenced to death, the punishment was never carried out.
Jackson v. Georgia, like Furman, was also a death penalty case confirmed by the Supreme Court of Georgia. Unlike Furman, however, the convicted man in Jackson had not killed anyone, but attempted to commit armed robbery and committed rape in the process of doing so. Branch v. Texas was brought to the Supreme Court of the United States on appeal on certiorari to the Texas Court of Criminal Appeals. Like Jackson, Branch was convicted of rape.[2]
Decision[edit]
In a 5–4 decision, the Court's one-paragraph per curiam opinion held that the imposition of the death penalty in these cases constituted cruel and unusual punishment and violated the Constitution.[3] However, the majority could not agree as to a rationale. There was no opinion of the court or plurality as none of the five justices constituting the majority joined in the opinion of any other.
Justices Potter Stewart, Byron White and William O. Douglas expressed similar concerns about the apparent arbitrariness with which death sentences were imposed under the existing laws, often indicating a racial bias against black defendants. Because these opinions were the narrowest, finding only that the death penalty as currently applied was cruel and unusual, they are often considered the controlling majority opinions. Stewart wrote:
These death sentences are cruel and unusual in the same way that being struck by lightning is cruel and unusual. For, of all the people convicted of rapes and murders in 1967 and 1968, many just as reprehensible as these, the petitioners are among a capriciously selected random handful upon whom the sentence of death has in fact been imposed. My concurring Brothers have demonstrated that, if any basis can be discerned for the selection of these few to be sentenced to death, it is the constitutionally impermissible basis of race. See McLaughlin v. Florida, 379 U.S. 184 (1964) But racial discrimination has not been proved, and I put it to one side. I simply conclude that the Eighth and Fourteenth Amendments cannot tolerate the infliction of a sentence of death under legal systems that permit this unique penalty to be so wantonly and so freakishly imposed.
Justices William Brennan and Thurgood Marshall concluded that the death penalty was in itself "cruel and unusual punishment," and incompatible with the evolving standards of decency of a contemporary society.
Dissents[edit]
Chief Justice Warren Burger and Justices Harry Blackmun, Lewis F. Powell, and William H. Rehnquist, each appointed by President Richard Nixon, dissented. They argued that a punishment provided in 40 state statutes (at the time) and by the federal government could not be ruled contrary to the so-called "evolving standard of decency."
Aftermath[edit]
The Furman decision caused all death sentences pending at the time to be reduced to life imprisonment, and it was described by scholars as a "legal bombshell."[4] The next day, columnist Barry Schweid wrote that it was "unlikely" that the death penalty could exist anymore in the United States.[5]
The Court's decision forced states and the U.S. Congress to rethink their statutes for capital offenses to ensure that the death penalty would not be administered in a capricious or discriminatory manner.[6]
In the following four years, 37 states enacted new death penalty laws aimed at overcoming the court's concerns about arbitrary imposition of the death penalty. Several statutes that mandated bifurcated trials, with separate guilt-innocence and sentencing phases, and imposing standards to guide the discretion of juries and judges in imposing capital sentences, were upheld in a series of Supreme Court decisions in 1976, led by Gregg v. Georgia. Other statutes enacted in response to Furman, such as Louisiana's which mandated imposition of the death penalty upon conviction of a certain crime, were struck down in cases of that same year.
See also[edit]
Capital punishment in the United States
List of United States Supreme Court cases, volume 408
Gregg v. Georgia
Baze v. Rees
Glossip v. Gross
References[edit]
^ Jump up to: a b Criminal Law - Cases and Materials, 7th ed. 2012, Wolters Kluwer Law & Business; John Kaplan, Robert Weisberg, Guyora Binder, ISBN 978-1-4548-0698-1, [1]
Jump up ^ "Branch v. Texas". TheFreeDictionary.com.
Jump up ^ Cornell University Law School. "Furman v. Georgia (No. 69-5003)". cornell.edu.
Jump up ^ Barry Latzer (2010), Death Penalty Cases: Leading U.S. Supreme Court Cases on Capital Punishment, Elsevier, p.37.
Jump up ^ The Free Lance-Star - Jun 30, 1972 : "New laws unlikely on death penalty," by Barry Schweid
Jump up ^ "Furman v. Georgia - The Oyez Project at IIT Chicago-Kent College of Law". oyez.org.
Further reading[edit]
Smith, Stephen F. (2008). "The Supreme Court and the Politics of Death". Virginia Law Review. 94 (2): 283–383. Archived from the original on 2009-04-04.
Hull, Elizabeth (January 2010). "Guilty On All Counts". Social Policy. 39 (4): 11–25, 15p.
External links[edit]
Furman v. Georgia, 408 U.S. 238 (1972) (full text with links to cited material)
Works related to Furman v. Georgia at Wikisource
Retrieved from "https://en.wikipedia.org/w/index.php?title=Furman_v._Georgia&oldid=804438627"
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American Civil Liberties Union litigation
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