WordNet
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/07/27 11:33:16」(JST)
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Mitochondrial ribosomal protein L31 |
Identifiers |
Symbol |
L31 |
Pfam |
PF09784 |
InterPro |
IPR016340 |
PROSITE |
PDOC00880 |
SCOP |
1m90 |
SUPERFAMILY |
1m90 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
A ribosomal protein is any of the proteins that, in conjunction with rRNA, make up the ribosomal subunits involved in the cellular process of translation. A large part of the knowledge about these organic molecules has come from the study of E. coli ribosomes. Most ribosomal proteins have been isolated and specific antibodies have been produced. These, together with electronic microscopy and the use of certain reactives, have allowed for the determination of the topography of the proteins in the ribosome.
Contents
- 1 Proteins in E. coli ribosomes
- 2 Disposition in the small ribosomal subunit
- 3 See also
- 4 References
- 5 External links
Proteins in E. coli ribosomes
The ribosome of E. coli has about 22 proteins in the small subunit (labelled S1 to S22) and 34 proteins in the large subunit (L1 to L36). All of them are different with three exceptions: one protein is found in both subunits (S20 and L26), L7 and L12 are acetylated and methylated forms of the same protein, and L8 is a complex of L7/L12 and L10. In addition, L31 is known to exist in two forms, the full length at 7.9 kilodaltons (kDa) and fragmented at 7.0 kDa. This is why the number of proteins in a ribosome is of 56. Except for S1 (with a molecular weight of 61.2 kDa), the other proteins range in weight between 4.4 and 29.7 kDa.[1]
Disposition in the small ribosomal subunit
In the small (30S) subunit of E. coli ribosomes, the proteins denoted S4, S7, S8, S15, S17, S20 bind independently to 16S rRNA. After assembly of these primary binding proteins, S5, S6, S9, S12, S13, S16, S18, and S19 bind to the growing ribosome. These proteins also potentiate the addition of S2, S3, S10, S11, S14, and S21. Protein binding to helical junctions is important for initiating the correct tertiary fold of RNA and to organize the overall structure. Nearly all the proteins contain one or more globular domains. Moreover, nearly all contain long extensions that can contact the RNA in far-reaching regions. Additional stabilization results from the proteins' basic residues, as these neutralize the charge repulsion of the RNA backbone. Protein-protein interactions also exist to hold structure together by electrostatic and hydrogen bonding interactions. Theoretical investigations pointed to correlated effects of protein-binding onto binding affinities during the assembly process [2]
See also
- Alpha operon ribosome binding site
- Ribosomal protein L20 leader
References
- ^ Arnold RJ, Reilly JP. (1999) "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Anal Biochem. v269(1): pp 105-12. PMID 10094780
- ^ Hamacher K, Trylska J, McCammon JA. (2006) "Dependency Map of Proteins in the Small Ribosomal Subunit." PLoS Comput. Biol. v2(2): e10. PMID 16485038
- De Robertis and De Robertis, Biología Celular y Molecular 10th ed., El Ateneo, Buenos Aires, 1982, ISBN 950-02-0027-9 (in Spanish)
- Monika Martick, Lucas H. Horan, Harry F. Noller and William G. Scott. A discontinuous hammerhead ribozyme embedded in a mammalian messenger RNA. doi:10.1038/nature07117
External links
- 30S Ribosomal proteins at biochem.umd.edu
- Ribosomal Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
Protein biosynthesis: translation (prokaryotic, eukaryotic)
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Ribosomal proteins |
Initiation factor |
Prokaryotic |
|
|
Archaeal |
|
|
Eukaryotic |
eIF1 |
|
|
eIF2 |
- EIF2S1
- EIF2S2
- EIF2S3
- EIF2B1
- EIF2B2
- EIF2B3
- EIF2B4
- EIF2B5
- EIF-2 kinase
|
|
eIF3 |
- EIF3A
- B
- C
- D
- F
- G
- H
- I
- J
- K
- M
- S6
|
|
eIF4 |
- EIF4A2
- A3
- B
- E1
- E2
- G1
- G2
- G3
- H
|
|
eIF5 |
|
|
eIF6 |
|
|
|
|
Elongation factor |
Prokaryotic |
|
|
Archaeal |
|
|
Eukaryotic |
- EEF-1
- EEF1A1
- EEF1A2
- EEF1A3
- EEF1B1
- EEF1B2
- EEF1B3
- EEF1B4
- EEF1D
- EEF1E1
- EEF1G
- EEF2
|
|
|
Release factor |
- Prokaryotic
- Archaeal
- Eukaryotic (ETF1)
|
|
Other |
- RPS1
- RPS2
- RPS3
- RPS4
- RPS5
- RPS6
- RPS7
- RPS8
- RPS9
- RPS10
- RPS11
- RPS12
- RPS13
- RPS14
- RPS15
- RPS16
- RPS17
- RPS18
- RPS19
- RPS20
- RPS21
- RPS22
- RPS23
- RPS24
- RPS25
- RPS26
- RPS27
- RPS28
- RPS29
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|
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Other concepts |
- Aminoacyl tRNA synthetase
- Reading frame
- Start codon
- Stop codon
- Shine-Dalgarno sequence/Kozak consensus sequence
|
|
see also disorders of translation and posttranslational modification
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)
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UpToDate Contents
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English Journal
- Development of qualitative and quantitative PCR analysis for meat adulteration from RNA samples.
- Cheng JH1, Chou HT2, Lee MS3, Sheu SC4.
- Food chemistry.Food Chem.2016 Feb 1;192:336-42. doi: 10.1016/j.foodchem.2015.06.094. Epub 2015 Jun 27.
- Total RNA samples were used to establish qualitative and quantitative PCR-based methods for assessing meat adulteration. The primers were designed based on the mRNA sequences of troponin I (TnI), mitochondrial ribosomal protein (MRP) and tropomodulin genes to distinguish chicken, pork, goat, beef an
- PMID 26304356
- Crystallographic Studies of the Ribosomal A-Site Molecular Switches by Using Model RNA Oligomers.
- Kondo J1.
- Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2016;1320:315-27. doi: 10.1007/978-1-4939-2763-0_20.
- An RNA molecular switch in the aminoacyl-tRNA decoding site (A site) of the ribosome plays a key role in the decoding process of the protein biosynthesis. The switch discriminates a single cognate-tRNA from near-cognate tRNAs by changing its conformation from "off" to "on" states and recognizing the
- PMID 26227052
- Reconstitution of Functionally Active Thermus thermophilus 30S Ribosomal Subunit from Ribosomal 16S RNA and Ribosomal Proteins.
- Agalarov S1, Yusupov M, Yusupova G.
- Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2016;1320:303-14. doi: 10.1007/978-1-4939-2763-0_19.
- In vitro reconstitution systems of ribosomal subunits from free ribosomal RNA and ribosomal proteins are helpful tool for studies on the structure, function and assembly of ribosome. Using this system mutant or modified ribosomal proteins or ribosomal RNA can be incorporated into ribosomal subunits
- PMID 26227051
Japanese Journal
- Direct interaction between EFL1 and SBDS is mediated by an intrinsically disordered insertion domain
- Asano Nozomi,Atsuumi Haruka,Nakamura Akiyoshi,Tanaka Yoshikazu,Tanaka Isao,Yao Min
- Biochemical and Biophysical Research Communications 443(4), 1251-1256, 2014-01-24
- … Removal of anti-association factor, Tif6 (eIF6), by elongation factor-like 1 (EFL1) and Shwachman-Bodian-Diamond syndrome (SBDS) protein is a critical step in the late stage of ribosome maturation. … Based on these observations together with those reported previously, we propose roles of EFL1 and SBDS in ribosomal maturation. …
- NAID 120005429607
- 4′,6-Dihydroxy-4-methoxyisoaurone Inhibits the HIF-1α Pathway Through Inhibition of Akt/mTOR/p70S6K/4E-BP1 Phosphorylation
- Mi Chunliu,Ma Juan,Shi Hui,Li Jing,Wang Fei,Lee Jung Joon,Jin Xuejun
- Journal of Pharmacological Sciences 125(2), 193-201, 2014
- … This compound markedly decreased the hypoxia-induced accumulation of HIF-1α protein dose-dependently, whereas it did not affect the expressions of HIF-1β and topoisomerase-I (Topo-I). …
- NAID 130004438624
- Evodiamine Inhibits Insulin-Stimulated mTOR-S6K Activation and IRS1 Serine Phosphorylation in Adipocytes and Improves Glucose Tolerance in Obese/Diabetic Mice
- Wang Ting,Kusudo Tatsuya,Takeuchi Tamaki,Yamashita Yukari,Kontani Yasuhide,Okamatsu Yuko,Saito Masayuki,Mori Nozomu,Yamashita Hitoshi
- PLoS ONE 8(12), e83264, 2013-12-31
- … There is a significant decrease in the mammalian target of rapamycin (mTOR) and ribosomal S6 protein kinase (S6K) signaling in white adipose tissue (WAT) in KK-Ay mice treated with evodiamine, in which glucose tolerance is improved. … Evodiamine also stimulates phosphorylation of AMP-activated protein kinase (AMPK), an important regulator of energy metabolism, which may cause down-regulation of mTOR signaling in adipocytes. …
- NAID 120005438864
Related Pictures
★リンクテーブル★
[★]
- 英
- ribosomal protein
- 関
- リボソーム
[★]
- 英
- ribosomal protein
- 関
- リボソーム
[★]
リボソームS6キナーゼ、リボソームタンパク質S6キナーゼ、S6リボソームキナーゼ、S6プロテインキナーゼ
- 関
- RSK、S6 kinase
[★]
90-kDaリボソームS6キナーゼ
- MAPキナーゼで活性化される細胞内シグナリング酵素
- 関
- p90 ribosomal S6 kinase
[★]
70-kDaリボソームS6キナーゼ
- 翻訳調節に関与するリン酸化酵素
- 関
- p70 S6 kinase、p70S6K
[★]
リボソームタンパク質S6
[★]
- 関
- ribosomally、ribosome