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Allosteric regulation
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Allosteric regulation of an enzyme
In biochemistry, allosteric regulation (or allosteric control) is the regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site.
The site to which the effector binds is termed the allosteric site or regulatory site. Allosteric sites allow effectors to bind to the protein, often resulting in a conformational change involving protein dynamics. Effectors that enhance the protein's activity are referred to as allosteric activators, whereas those that decrease the protein's activity are called allosteric inhibitors.
Allosteric regulations are a natural example of control loops, such as feedback from downstream products or feedforward from upstream substrates. Long-range allostery is especially important in cell signaling.[1] Allosteric regulation is also particularly important in the cell's ability to adjust enzyme activity.
The term allostery comes from the Greek allos (ἄλλος), "other", and stereos (στερεὀς), "solid (object)". This is in reference to the fact that the regulatory site of an allosteric protein is physically distinct from its active site.
Contents
[hide]
1 Models
1.1 Concerted model
1.2 Sequential model
1.3 Morpheein model
1.4 Ensemble models
2 Allosteric modulation
3 Energy sensing model
3.1 Positive modulation
3.2 Negative modulation
4 Types
4.1 Homotropic
4.2 Heterotropic
4.3 Essential activators
5 Non-regulatory allostery
6 Pharmacology
6.1 Allosteric sites as drug targets
7 Synthetic allosteric systems
8 Online resources
8.1 Allosteric database
8.2 Allosteric residues and their prediction using the STRESS web server
9 See also
10 References
11 External links
Models[edit]
A – Active site
B – Allosteric site
C – Substrate
D – Inhibitor
E – Enzyme
This is a diagram of allosteric regulation of an enzyme.
Many allosteric effects can be explained by the concerted MWC model put forth by Monod, Wyman, and Changeux,[2] or by the sequential model described by Koshland, Nemethy, and Filmer.[3] Both postulate that protein subunits exist in one of two conformations, tensed (T) or relaxed (R), and that relaxed subunits bind substrate more readily than those in the tense state. The two models differ most in their assumptions about subunit interaction and the preexistence of both states. For proteins in which subunits exist in more than two conformations, the allostery landscape model described by Cuendet, Weinstein, and LeVine,[4] can be used.
Concerted model[edit]
The concerted model of allostery, also referred to as the symmetry model or MWC model, postulates that enzyme subunits are connected in such a way that a conformational change in one subunit is necessarily conferred to all other subunits. Thus, all subunits must exist in the same conformation. The model further holds that, in the absence of any ligand (substrate or otherwise), the equilibrium favors one of the conformational states, T or R. The equilibrium can be shifted to the R or T state through the binding of one ligand (the allosteric effector or ligand) to a site that is different from the active site (the allosteric site).
Sequential model[edit]
The sequential model of allosteric regulation holds that subunits are not connected in such a way that a conformational change in one induces a similar change in the others. Thus, all enzyme subunits do not necessitate the same conformation. Moreover, the sequential model dictates that molecules of a substrate bind via an induced fit protocol. In general, when a subunit randomly collides with a molecule of substrate, the active site, in essence, forms a glove around its substrate. While such an induced fit converts a subunit from the tensed state to relaxed state, it does not propagate the conformational change to adjacent subunits. Instead, substrate-binding at one subunit only slightly alters the structure of other subunits so that their binding sites are more receptive to substrate. To summarize:
subunits need not exist in the same conformation
molecules of substrate bind via induced-fit protocol
conformational changes are not propagated to all subunits
Morpheein model[edit]
The morpheein model of allosteric regulation is a dissociative concerted model.[5]
A morpheein is a homo-oligomeric structure that can exist as an ensemble of physiologically significant and functionally different alternate quaternary assemblies. Transitions between alternate morpheein assemblies involve oligomer dissociation, conformational change in the dissociated state, and reassembly to a different oligomer. The required oligomer disassembly step differentiates the morpheein model for allosteric regulation from the classic MWC and KNF models.
Porphobilinogen synthase (PBGS) is the prototype morpheein.
Ensemble models[edit]
Ensemble models of allosteric regulation enumerate an allosteric system's statistical ensemble as a function of its potential energy function, and then relate specific statistical measurements of allostery to specific energy terms in the energy function (such as an intermolecular salt bridge between two domains).[6] Ensemble models like the ensemble allosteric model[7] and allosteric Ising model[8] assume that each domain of the system can adopt two states similar to the MWC model. The allostery landscape model introduced by Cuendet, Weinstein, and LeVine.[4] allows for the domains to have any number of states and the contribution of a specific molecular interaction to a given allosteric coupling can be estimated using a rigorous set of rules. Molecular dynamics simulations can be used to estimate a system's statistical ensemble so that it can be analyzed with the allostery landscape model.
Allosteric modulation[edit]
Main article: Allosteric modulator
Allosteric modulation is commonly used to alter the activity of molecules and enzymes in biochemistry and pharmacology. For example, drugs are made to bind to the active site of the enzyme which inhibit the substrates to bind to the enzyme and perform the reaction. Allosteric modulation occurs when a specific ligand binds to the allosteric site (also known as the regulatory site) of the enzyme and alters the drugs' effects on the substrates by either activating or inhibiting the enzyme activity. Allosteric modulators are designed to fit the allosteric site to cause conformational changes of the enzyme by changing the shape of the active site which causes a change in its activity. They work regardless of the fact that the enzyme substrate was able to bind to the active site or not. They can be positive,(activating) causing an increase of the enzyme activity, or they can be negative (inhibiting) causing a decrease of the enzyme activity. The use of allosteric modulation allows the control of the effects of specific enzyme activities, as a result, allosteric modulators are very effective in pharmacology.[9]
Energy sensing model[edit]
An example of this model is seen with the Mycobacterium tuberculosis, a bacterium that is perfectly suited to adapt to living in the macrophages of humans. The enzyme's sites serve as a communication between different substrates. Specifically between AMP and G6P. Sites like these also serve as a sensing mechanism for the enzyme's performance.[10]
Positive modulation[edit]
Positive allosteric modulation (also known as allosteric activation) occurs when the binding of one ligand enhances the attraction between substrate molecules and other binding sites. An example is the binding of oxygen molecules to hemoglobin, where oxygen is effectively both the substrate and the effector. The allosteric, or "other", site is the active site of an adjoining protein subunit. The binding of oxygen to one subunit induces a conformational change in that subunit that interacts with the remaining active sites to enhance their oxygen affinity. Another example of allosteric activation is seen in cytosolic IMP-GMP specific 5'-nucleotidase II (cN-II), where the affinity for substrate GMP increases upon GTP binding at the dimer interface[11]
Negative modulation[edit]
Negative allosteric modulation (also known as allosteric inhibition) occurs when the binding of one ligand decreases the affinity for substrate at other active sites. For example, when 2,3-BPG binds to an allosteric site on hemoglobin, the affinity for oxygen of all subunits decreases. This is when a regulator is absent from the binding site.
Direct thrombin inhibitors provides an excellent example of negative allosteric modulation. Allosteric inhibitors of thrombin have been discovered which could potentially be used as anticoagulants.
Another example is strychnine, a convulsant poison, which acts as an allosteric inhibitor of the glycine receptor. Glycine is a major post-synaptic inhibitory neurotransmitter in mammalian spinal cord and brain stem. Strychnine acts at a separate binding site on the glycine receptor in an allosteric manner; i.e., its binding lowers the affinity of the glycine receptor for glycine. Thus, strychnine inhibits the action of an inhibitory transmitter, leading to convulsions.
Another instance in which negative allosteric modulation can be seen is between ATP and the enzyme phosphofructokinase within the negative feedback loop that regulates glycolysis. Phosphofructokinase (generally referred to as PFK) is an enzyme that catalyses the third step of glycolysis: the phosphorylation of fructose-6-phosphate into fructose 1,6-bisphosphate. PFK can be allosterically inhibited by high levels of ATP within the cell. When ATP levels are high, ATP will bind to an allosteoric site on phosphofructokinase, causing a change in the enzyme's three-dimensional shape. This change causes its affinity for substrate (fructose-6-phosphate and ATP) at the active site to decrease, and the enzyme is deemed inactive. This causes glycolysis to cease when ATP levels are high, thus conserving the body's glucose and maintaining balanced levels of cellular ATP. In this way, ATP serves as a negative allosteric modulator for PFK, despite the fact that it is also a substrate of the enzyme.
Types[edit]
Homotropic[edit]
A homotropic allosteric modulator is a substrate for its target enzyme, as well as a regulatory molecule of the enzyme's activity. It is typically an activator of the enzyme. For example, O2 and CO are homotropic allosteric modulators of hemoglobin.
Heterotropic[edit]
A heterotropic allosteric modulator is a regulatory molecule that is not the enzyme's substrate. It may be either an activator or an inhibitor of the enzyme. For example, H+, CO2, and 2,3-bisphosphoglycerate are heterotropic allosteric modulators of hemoglobin.[12]
Some allosteric proteins can be regulated by both their substrates and other molecules. Such proteins are capable of both homotropic and heterotropic interactions.
Essential activators[edit]
Some allosteric activators are referred to as "essential", or "obligate" activators, in the sense that in their absence, the activity of their target enzyme activity is very low or negligible, as is the case with N-acetylglutamate's activity on carbamoyl phosphate synthetase I, for example.[13][14]
Non-regulatory allostery[edit]
A non-regulatory allosteric site is any non-regulatory component of an enzyme (or any protein), that is not itself an amino acid. For instance, many enzymes require sodium binding to ensure proper function. However, the sodium does not necessarily act as a regulatory subunit; the sodium is always present and there are no known biological processes to add/remove sodium to regulate enzyme activity. Non-regulatory allostery could comprise any other ions besides sodium (calcium, magnesium, zinc), as well as other chemicals and possibly vitamins.
Pharmacology[edit]
Allosteric modulation of a receptor results from the binding of allosteric modulators at a different site (a "regulatory site") from that of the endogenous ligand (an "active site") and enhances or inhibits the effects of the endogenous ligand. Under normal circumstances, it acts by causing a conformational change in a receptor molecule, which results in a change in the binding affinity of the ligand. In this way, an allosteric ligand modulates the receptor's activation by its primary (orthosteric) ligand, and can be thought to act like a dimmer switch in an electrical circuit, adjusting the intensity of the response.
For example, the GABAA receptor has two active sites that the neurotransmitter gamma-aminobutyric acid (GABA) binds, but also has benzodiazepine and general anaesthetic agent regulatory binding sites. These regulatory sites can each produce positive allosteric modulation, potentiating the activity of GABA. Diazepam is an agonist at the benzodiazepine regulatory site, and its antidote flumazenil is an antagonist.
More recent examples of drugs that allosterically modulate their targets include the calcium-mimicking cinacalcet and the HIV treatment maraviroc.
Allosteric sites as drug targets[edit]
Allosteric sites may represent a novel drug target. There are a number of advantages in using allosteric modulators as preferred therapeutic agents over classic orthosteric ligands. For example, G protein-coupled receptor (GPCR) allosteric binding sites have not faced the same evolutionary pressure as orthosteric sites to accommodate an endogenous ligand, so are more diverse.[15] Therefore, greater GPCR selectivity may be obtained by targeting allosteric sites.[15] This is particularly useful for GPCRs where selective orthosteric therapy has been difficult because of sequence conservation of the orthosteric site across receptor subtypes.[16] Also, these modulators have a decreased potential for toxic effects, since modulators with limited co-operativity will have a ceiling level to their effect, irrespective of the administered dose.[15] Another type of pharmacological selectivity that is unique to allosteric modulators is based on co-operativity. An allosteric modulator may display neutral co-operativity with an orthosteric ligand at all subtypes of a given receptor except the subtype of interest, which is termed "absolute subtype selectivity".[16] If an allosteric modulator does not possess appreciable efficacy, it can provide another powerful therapeutic advantage over orthosteric ligands, namely the ability to selectively tune up or down tissue responses only when the endogenous agonist is present.[16] Oligomer-specific small molecule binding sites are drug targets for medically relevant morpheeins.[17]
Synthetic allosteric systems[edit]
There are many synthetic compounds containing several noncovalent binding sites, which exhibit conformational changes upon occupation of one site. Cooperativity between single binding contributions in such supramolecular systems is positive if occupation of one binding site enhances the affinity ΔG at a second site, and negative if the affinity is lowered. Most synthetic allosteric complexes rely on conformational reorganization upon the binding of one effector ligand which then leads to either enhanced or weakened association of second ligand at another binding site.[18][19][20] Conformational coupling between several binding sites is in artificial systems usually much larger than in proteins with their usually larger flexibility. The parameter which determines the efficiency (as measured by the ratio of equilibrium constants Krel = KA(E)/KA in presence and absence of an effector E ) is the conformational energy needed to adopt a closed or strained conformation for the binding of a ligand A.[21]
In many multivalentsupramolecular systems[22] direct interaction between bound ligands can occur, which can lead to large cooperativities. Most common is such a direct interaction between ions in receptors for ion-pairs.[23][24] This cooperatitiy is often also referred to as allostery, even though conformational changes here are not necessarily triggering binding events.
Online resources[edit]
Allosteric database[edit]
Allostery is a direct and efficient means for regulation of biological macromolecule function, produced by the binding of a ligand at an allosteric site topographically distinct from the orthosteric site. Due to the often high receptor selectivity and lower target-based toxicity, allosteric regulation is also expected to play an increasing role in drug discovery and bioengineering. The AlloSteric Database (ASD, http://mdl.shsmu.edu.cn/ASD)[25] provides a central resource for the display, search and analysis of the structure, function and related annotation for allosteric molecules. Currently, ASD contains allosteric proteins from more than 100 species and modulators in three categories (activators, inhibitors, and regulators). Each protein is annotated with detailed description of allostery, biological process and related diseases, and each modulator with binding affinity, physicochemical properties and therapeutic area. Integrating the information of allosteric proteins in ASD should allow the prediction of allostery for unknown proteins, to be followed with experimental validation. In addition, modulators curated in ASD can be used to investigate potential allosteric targets for a query compound, and can help chemists to implement structure modifications for novel allosteric drug design.
Allosteric residues and their prediction using the STRESS web server[edit]
Not all protein residues play equally important roles in allosteric regulation. The identification of residues that are essential to allostery (so-called “allosteric residues”) has been the focus of many studies, especially within the last decade.[26][27][28][29][30][31][32][33] In part, this growing interest is a result of their general importance in protein science, but also because allosteric residues may be exploited in biomedical contexts. Pharmacologically important proteins with difficult-to-target sites may yield to approaches in which one alternatively targets easier-to-reach residues that are capable of allosterically regulating the primary site of interest. These residues can broadly be classified as surface- and interior-allosteric amino acids. Allosteric sites at the surface generally play regulatory roles that are fundamentally distinct from those within the interior; surface residues may serve as receptors or effector sites in allosteric signal transmission, whereas those within the interior may act to transmit such signals. STRucturally-identified ESSential residues (STRESS, http://stress.molmovdb.org) is a web tool that enables users to submit their own protein structures of interest in order to predict both surface- and interior-allosteric residues in an algorithmically efficient manner.[34] The software behind this server employs 3D structures to build models of conformational change in order to perform predictions.
See also[edit]
ASD database
Competitive inhibition
Cooperative binding
Enzyme kinetics
Protein dynamics
Receptor theory
References[edit]
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Jump up ^ Gasper PM, Fuglestad B, Komives EA, Markwick PR, McCammon JA (December 2012). "Allosteric networks in thrombin distinguish procoagulant vs. anticoagulant activities". Proceedings of the National Academy of Sciences of the United States of America. 109 (52): 21216–22. doi:10.1073/pnas.1218414109. PMC 3535651  . PMID 23197839.
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External links[edit]
Instant insight introducing a classification system for protein allostery mechanisms from the Royal Society of Chemistry
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Rajya Sabha
From Wikipedia, the free encyclopedia
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For Current list of Rajya Sabha members, see List of current members of the Rajya Sabha.
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Coordinates: 28°37′0″N 77°12′30″E / 28.61667°N 77.20833°E / 28.61667; 77.20833
Rajya Sabha
Council of States
Emblem of India
Type
Type
Upper house of the Parliament of India
Term limits
6 years
Leadership
Chairman
(Vice-President)
Venkaiah Naidu[1]
Since 11 August 2017
Deputy Chairman
Vacant
Since 1 July 2018
Leader of the House
Arun Jaitley, BJP
Since 2 June 2014[2]
Leader of the Opposition
Ghulam Nabi Azad, INC
Since 8 June 2014[2]
Structure
Seats
245
233 Elected
12 Nominated
1 Vacant (1 Elected Seat)[3]
Political groups
Government coalition (87)
National Democratic Alliance (87)
BJP (71)
JD(U) (6)
SAD (3)
SS (3)
BPF (1)
NPF (1)
RPI(A) (1)
SDF (1)
Opposition Parties (158)
United Progressive Alliance (57)
INC (50)
DMK (4)
IUML (1)
JD(S) (1)
KC(M) (1)
Janata Parivar Parties (6)
RJD (5)
INLD (1)
Unaligned Parties (82)
AIADMK (13)
AITC (13)
SP (13)
BJD (9)
TDP (6)
TRS (6)
CPI(M) (5)
BSP (4)
NCP (4)
AAP (3)
CPI (2)
JKPDP (2)
YSRCP (2)
Others (13)
Nominated (6)
Independents (6)
Vacant (1)
Elections
Voting system
Single transferable vote
Last election
16 January, 23 March and 21 June 2018
Meeting place
Chamber of Rajya Sabha, Sansad Bhavan,
Sansad Marg, New Delhi, India
Website
rajyasabha.nic.in
The Rajya Sabha or Council of States is the upper house of the Parliament of India. Membership of Rajya Sabha is limited by the Constitution to a maximum of 250 members, and current laws have provision for 245 members. Most of the members of the House are indirectly elected by state and territorial legislatures using single transferable votes, while the President can appoint 12 members for their contributions to art, literature, science, and social services. Members sit for staggered six-year terms, with one third of the members retiring every two years.[4]
The Rajya Sabha meets in continuous sessions, and unlike the Lok Sabha, the lower house of Parliament, is not subject to dissolution. However, the Rajya Sabha, like the Lok Sabha can be prorogued by the President. The Rajya Sabha has equal footing in all areas of legislation with Lok Sabha, except in the area of supply, where the Lok Sabha has overriding powers. In the case of conflicting legislation, a joint sitting of the two houses can be held. However, since the Lok Sabha has twice as many members as the Rajya Sabha, the former would normally hold the greater power. Joint sittings of the Houses of Parliament of India are rare, and in the history of the Republic, only three such joint-sessions have been held; the latest one for the passage of the 2002 Prevention of Terrorism Act.
The Vice President of India (currently, Venkaiah Naidu) is the ex-officio Chairman of the Rajya Sabha, who presides over its sessions. The Deputy Chairman, who is elected from amongst the house's members, takes care of the day-to-day matters of the house in the absence of the Chairman. The Rajya Sabha held its first sitting on 13 May 1952.[5] The salary and other benefits for a member of Rajya Sabha are same as for a member of Lok Sabha.
Rajya Sabha members are elected by state legislatures rather than directly through the electorate by single transferable vote method.
Contents
[hide]
1 Qualifications
2 Limitations
2.1 Money bills
2.2 Joint Sitting of the Parliament
2.3 No-confidence motion
3 Powers
3.1 Union-States Relations
3.2 Creation of All-India Services
4 Membership and Composition
4.1 List of constituencies by States/Union Territories
4.2 Membership by party
5 Officers
5.1 Leader of the House
5.2 Leader of the Opposition
6 Secretariat
7 Media
8 See also
9 References
10 Further reading
11 External links
Qualifications[edit]
Article 84 of the Constitution lays down the qualifications for membership of Parliament. A member of the Rajya Sabha must:[6]
Be a citizen of India.
Make and subscribe before some person authorized in that behalf by the Election Commission an oath or affirmation according to the form set out for the purpose in the Third Schedule to the Constitution.
Be at least 30 years old.
Be elected by the Legislative Assembly of States and Union territories by means of Single transferable vote through Proportional representation.[7]
Not be a proclaimed criminal.
Not be an insolvent, i.e. he/she should not be in debt that he/she is not capable of repaying in a current manner and should have the ability to meet his/her financial expenses.
Not hold any other office of profit under the Government of India.
Not be of unsound mind.
Possess such other qualifications as may be prescribed in that behalf by or under any law made by Parliament.
In addition, twelve members are nominated by the President of India having special knowledge in various areas like arts and science. However, they are not entitled to vote in Presidential elections as per Article 55 of the Constitution.
Limitations[edit]
The Constitution of India places some restrictions on Rajya Sabha which makes Lok Sabha more powerful in certain areas in comparison.
Money bills[edit]
The definition of a money bill is given in article 110 of constitution of India. A money bill can be introduced only in the Lok Sabha by a minister and only on recommendation of President of India. When the Lok Sabha passes a money bill then the Lok Sabha sends money bill to the Rajya Sabha council of states for 14 days during which it can make recommendations. Even if Rajya Sabha fails to return the money bill in 14 days to the Lok Sabha, that bill is deemed to have passed by both the Houses. Also, if the Lok Sabha rejects any (or all) of the amendments proposed by the Rajya Sabha, the bill is deemed to have been passed by both Houses of Parliament of India in the form the Lok Sabha finally passes it. This is because the Lok Sabha has largest number of representatives of peoples of India and so the Lok Sabha lower house also called house of the peoples is more powerful in comparison with Rajya Sabha council of states upper house. Hence, Rajya Sabha can only give recommendations for a money bill but Rajya Sabha cannot amend a money bill this is to ensure that Rajya Sabha must not add any non money matters in money bill. Lok Sabha can reject all the recommendations of Rajya Sabha or can accept some or all of the recommendations. Decisions of the speaker of the Lok Sabha are final. There is no joint sitting of both the houses with respect to money bills, because all final decisions are taken by the Lok Sabha.[8]
Joint Sitting of the Parliament[edit]
Article 108 provides for a joint sitting of the two Houses of Parliament in certain cases. A joint sitting can be convened by the President of India when one house has either rejected a bill passed by the other house, has not taken any action on a bill transmitted to it by the other house for six months, or has disagreed to the amendments proposed by the Lok Sabha on a bill passed by it. Considering that the numerical strength of Lok Sabha is more than twice that of Rajya Sabha, Lok Sabha tends to have a greater influence in a joint sitting of Parliament. A joint session is chaired by the Speaker of Lok Sabha. Also, because the joint session is convened by the President on advice of the government, which already has a majority in Lok Sabha, the joint session is usually convened to get bills passed through a Rajya Sabha in which the government has a minority.
Joint sessions of Parliament are a rarity, and have been convened three times in last 71 years, for the purpose of passage of a specific legislative act, the latest time being in 2002:
1961: Dowry Prohibition Act, 1958
1978: Banking Services Commission (Repeal) Act, 1977
2002: Prevention of Terrorism Act, 2002
No-confidence motion[edit]
Unlike the Lok Sabha, a member of the Rajya Sabha cannot bring to the house a no-confidence motion against the government.
Powers[edit]
In Indian federal structure, Rajya Sabha is a representative of the States in the Union legislature (Hence the name, Council of States). Hence, Rajya Sabha is granted powers that protect the rights of States against the Union.
Union-States Relations[edit]
The Constitution empowers Parliament of India to make laws on the matters reserved for States (States List). However, this can only be done if Rajya Sabha first passes a resolution by two-thirds special majority granting such a power to the Union Parliament. The union government cannot make a law on a matter reserved for states without any authorisation from Rajya Sabha.
Creation of All-India Services[edit]
Rajya Sabha, by a two-thirds super majority can pass a resolution empowering the Government of India to create more All-India Services common to both Union and States, including a judicial service.
Membership and Composition[edit]
Seats are allotted in proportion to the population of people of each state or union territory in such a manner that smaller states have slight advantage over more populous states.[9] As the members are elected by the state legislature, smaller Union Territories which are not States and do not have legislatures cannot have representation in Rajya Sabha. Hence, Andaman & Nicobar Islands, Lakshadweep, Chandigarh, Daman & Diu and Dadra & Nagar Haveli do not send any representatives to Rajya Sabha. 12 members are nominated by the President.[10][11]
As per the Fourth Schedule to the Constitution of India on 26 January 1950, the Rajya Sabha was to consist of 216 members of which 12 members were to be nominated by the President and the remaining 204 elected to represent the States.[11] The present strength, however, is 245 members of whom 233 are representatives of the states and union territories and 12 are nominated by the President.[11] The twelve nominated members of the Rajya Sabha are persons who are eminent in particular fields, and are well known contributors in the particular field. A few examples of such nominated persons are cricketing icon Sachin Tendulkar, former RBI Governor Bimal Jalan and famous lyricist and poet Javed Akhtar. As of March 2014, each state or union territory specified in the first column of the following table, there shall be allotted the number of seats specified in the second column thereof opposite to that State or that union territory, as the case may be:[12]
List of constituencies by States/Union Territories[edit]
Name of state and union territory
No. of Seats
Andhra Pradesh[13] 11
Arunachal Pradesh 1
Assam 7
Bihar 16
Chhattisgarh 5
Goa 1
Gujarat 11
Haryana 5
Himachal Pradesh 3
Jammu & Kashmir 4
Jharkhand 6
Karnataka 12
Kerala 9
Madhya Pradesh 11
Maharashtra 19
Manipur 1
Meghalaya 1
Mizoram 1
Nagaland 1
National Capital Territory of Delhi 3
Nominated 12
Odisha 10
Puducherry 1
Punjab 7
Rajasthan 10
Sikkim 1
Tamil Nadu 18
Telangana[13] 7
Tripura 1
Uttar Pradesh 31
Uttarakhand 3
West Bengal 16
Total 245
Membership by party[edit]
Main article: List of current members of the Rajya Sabha
Rajya Sabha Secretariat (As of 15 July 2018):[14]
Alliances
Party
MP
National Democratic Alliance
Seats: 87 Bharatiya Janata Party 71
Janata Dal (United) 6
Shiromani Akali Dal 3
Shiv Sena 3
Bodoland People's Front 1
Naga People's Front 1
Republican Party of India (A) 1
Sikkim Democratic Front 1
United Progressive Alliance
Seats: 57 Indian National Congress 50
Dravida Munnetra Kazhagam 4
Indian Union Muslim League 1
Janata Dal (Secular) 1
Kerala Congress (M) 1
Janata Parivar
Seats: 6 Rashtriya Janata Dal 5
Indian National Lok Dal 1
Other Parties
Seats: 82 All India Anna Dravida Munnetra Kazhagam 13
All India Trinamool Congress 13
Samajwadi Party 13
Biju Janata Dal 9
Telugu Desam Party 6
Telangana Rashtra Samithi 6
Communist Party of India (Marxist) 5
Bahujan Samaj Party 4
Nationalist Congress Party 4
Aam Aadmi Party 3
Communist Party of India 2
Jammu and Kashmir Peoples Democratic Party 2
YSR Congress Party 2
Nominated 6
Independents 6
Vacant Seats 1 Seat from Bihar 1
Total 245
Officers[edit]
Leader of the House[edit]
Main article: Leader of the House (Rajya Sabha)
Besides the Chairman (Vice-President of India) and the Deputy Chairman, there is also a position called Leader of the House. This is a cabinet minister – the prime minister if he is a member of the House, or another nominated minister. The Leader has a seat next to the Chairman, in the front row.
Leader of the Opposition[edit]
Main article: Leader of the Opposition (India)
Besides the Leader of the House, who is leading the majority, there is also a Leader of the Opposition (LOP) – leading the opposition parties. The function was only recognized in the Salary and Allowances of Leaders of the Opposition in Parliament Act 1977. This is commonly the leader of the largest non-government party, and is recognized as such by the Chairman.
The following people have been the Leader of the Opposition in the Rajya Sabha:
Sr No
Name
Portrait
Term of office
Political party
(Alliance)
Prime Minister
1 Shyam Nandan Mishra December 1969 March 1971 INC (O) Indira Gandhi
2 M. S. Gurupadaswamy March 1971 April 1972
3 Kamalapati Tripathi 30 March 1977 15 February 1978 INC Morarji Desai
4 Bhola Paswan Shastri 24 February 1978 23 March 1978 INC (O)
5 Kamalapati Tripathi 23 March 1978 8 January 1980 INC
Charan Singh
6 Lal Krishna Advani 21 January 1980 7 April 1980 Janata Party Indira Gandhi
7 P. Shiv Shankar 18 December 1989 2 January 1991 INC V. P. Singh
Chandra Shekhar
8 M. S. Gurupadaswamy 28 June 1991 21 July 1991 Janata Dal P. V. Narasimha Rao
9 S. Jaipal Reddy 22 July 1991 29 June 1992
10 Sikander Bakht 7 July 1992 23 May 1996 BJP
11 Shankarrao Chavan 23 May 1996 1 June 1996 INC Atal Bihari Vajpayee
12 Sikander Bakht 1 June 1996 19 March 1998 BJP H. D. Deve Gowda
I. K. Gujral
13 Manmohan Singh 21 March 1998 21 May 2004 INC Atal Bihari Vajpayee
14 Jaswant Singh 3 June 2004 16 May 2009 BJP Manmohan Singh
15 Arun Jaitley 3 June 2009 26 May 2014
16 Ghulam Nabi Azad 8 June 2014 Incumbent INC Narendra Modi
Secretariat[edit]
The Secretariat of Rajya Sabha was set up pursuant to the provisions contained in Article 98 of the Constitution. The said Article, which provides for a separate secretarial staff for each House of Parliament, reads as follows:- 98. Secretariat of Parliament – Each House of Parliament shall have a separate secretarial staff: Provided that nothing in this clause shall be construed as preventing the creation of posts common to both Houses of Parliament. (2) Parliament may by law regulate the recruitment and the conditions of service of persons appointed to the secretarial staff of either House of Parliament.
The Rajya Sabha Secretariat functions under the overall guidance and control of the Chairman. The main activities of the Secretariat inter alia include the following :
(i) providing secretarial assistance and support to the effective functioning of the Council of States (Rajya Sabha) possible to Members of Rajya Sabha; (iv) servicing the various Parliamentary Committees; (v) preparing research and reference material and bringing out various publications; (vi) recruitment of manpower in the Sabha Secretariat and attending to personnel matters; and (vii) preparing and publishing a record of the day-to-day proceedings of the Rajya Sabha and bringing out such other publications, as may be required concerning the functioning of the Rajya Sabha and its Committees.
In the discharge of his constitutional and statutory responsibilities, the Chairman, Rajya Sabha is assisted by the Secretary-General, who holds the rank equivalent[16] to the Cabinet Secretary to the Government of India. The Secretary-General, in turn, is assisted by senior functionaries at the level of Secretary, Additional Secretary, Joint Secretary and other officers and staff of the Secretariat. Present secretary-general is Desh Deepak Sharma, IAS. [15]
Media[edit]
Rajya Sabha Television (RSTV) is a 24-hour a day, seven day a week parliamentary TV channel fully owned and operated by the Rajya Sabha. The channel is aimed at providing in-depth coverage and analysis of parliamentary affairs especially the functioning of and developments related to Rajya Sabha. During sessions of Parliament, apart from telecasting live coverage of the proceedings of Rajya Sabha, RSTV presents incisive analysis of the proceedings of the House as well as other day-to-day parliamentary events and developments.[16]
See also[edit]
List of current members of the Rajya Sabha
Parliament of India
Lok Sabha
References[edit]
Jump up ^ "Venkaiah Naidu sworn in as Vice-President". The Hindu. New Delhi, India. 11 August 2017. Archived from the original on 9 February 2014.
^ Jump up to: a b "RAJYA SABHA – AN INTRODUCTION". rajyasabha.nic.in. Archived from the original on 16 August 2011.
Jump up ^ "MEMBERS OF RAJYA SABHA (STATE WISE LIST)". Rajya Sabha. 28 June 2018. Archived from the original on 5 February 2014.
Jump up ^ Deshmukh, Yashwant (11 June 2016). "Crucial polls today: A guide to calculus of Rajya Sabha for dummies". Firstpost. Archived from the original on 19 June 2016. Retrieved 20 June 2016.
Jump up ^ "OUR PARLIAMENT". Indian Parliament. Archived from the original on 17 May 2011. Retrieved 11 May 2011.
Jump up ^ "Council of States (Rajya Sabha) – rajyasabha.in". Archived from the original on 18 June 2012.
Jump up ^ "HANDBOOK FOR RETURNING OFFICERS – FOR ELECTIONS TO THE COUNCIL OF STATES AND STATE LEGISLATIVE COUNCILS" (PDF). Election Commission of India. 1992. pp. 400–426. Archived (PDF) from the original on 10 January 2017. Retrieved 2 August 2017.
Jump up ^ "Website of the Rajya Sabha – Legislation".
Jump up ^ "642 Sidharth Chauhan, Bicameralism: comparative insights and lessons". Archived from the original on 18 May 2015. Retrieved 15 May 2015.
Jump up ^ "FREQUENTLY ASKED QUESTIONS ABOUT RAJYA SABHA". Indian Parliament. Archived from the original on 24 July 2013. Retrieved 8 December 2012.
^ Jump up to: a b c "Composition of Rajya Sabha – Rajya Sabha At Work" (PDF). rajyasabha.nic.in. Rajya Sabha Secretariat, New Delhi. Archived from the original (PDF) on 5 March 2016. Retrieved 20 October 2015.
Jump up ^ "Fourth Schedule" (PDF). Ministry of Law. Archived (PDF) from the original on 26 July 2015. Retrieved 18 May 2015. This article incorporates text from this source, which is in the public domain.
^ Jump up to: a b "Rajya Sabha members alloted [sic] to Telangana, Andhra Pradesh". The Economic Times. 30 May 2014. Archived from the original on 9 February 2014. Retrieved 21 October 2015.
Jump up ^ "STRENGTHWISE PARTY POSITION IN THE RAJYA SABHA". Rajya Sabha. 28 June 2018. Archived from the original on 6 June 2017.
Jump up ^ http://164.100.47.5/newsite/rssorgchart/sg.aspx
Jump up ^ "About Rajya Sabha TV". Rajya Sabha. Archived from the original on 9 February 2014. Retrieved 19 May 2014.
Further reading[edit]
The Nominated Members of India's Council of States: A Study of Role-Definition J. H. Proctor, Legislative Studies Quarterly, Vol. 10, No. 1, Feb 1985, pp. 53–70.
Alistair, McMillan. "Constitution 91st Amendment Bill: A Constitutional Fraud?". nuff.ox.ac.uk. Retrieved 19 May 2014.
External links[edit]
Rajya Sabha homepage hosted by the Indian government
Rajya Sabha FAQ page hosted by the Indian government
37 Rajya Sabha members have criminal background: Study – analysis by the Association for Democratic Reforms and National Election Watch
Nominated members list
State wise list
Rajya Sabha Television
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