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InterPro: IPR002583 Ribosomal protein S20
Protein matches
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UniProtKB Matches: 1682 proteins |
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Accession
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IPR002583 Ribosomal_S20 |
Secondary
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IPR010013
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Type
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Family |
Signatures
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GO Term annotation
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Process
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GO:0006412 translation
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Function
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GO:0003723 RNA binding
GO:0003735 structural constituent of ribosome
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Component
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GO:0005622 intracellular
GO:0005840 ribosome
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [1, 2]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.
Many of ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [2, 3].
This family consists of bacterial (and chloroplast) examples of the ribosomal small subunit protein S20. Bacterial ribosomal protein S20 forms part of the 30S ribosomal subunit, and interacts with 16S rRNA.
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Structural links
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Database links
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Additional Reading
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Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller HF.
Structural basis for translation termination on the 70S ribosome.
Nature 454 2008 852-7
[PubMed: 18596689]
http://dx.doi.org/10.1038/nature07115
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Kurata S, Weixlbaumer A, Ohtsuki T, Shimazaki T, Wada T, Kirino Y, Takai K, Watanabe K, Ramakrishnan V, Suzuki T.
Modified uridines with C5-methylene substituents at the first position of the tRNA anticodon stabilize U.G wobble pairing during decoding.
J. Biol. Chem. 283 2008 18801-11
[PubMed: 18456657]
http://dx.doi.org/10.1074/jbc.M800233200
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Stern S, Changchien LM, Craven GR, Noller HF.
Interaction of proteins S16, S17 and S20 with 16 S ribosomal RNA.
J. Mol. Biol. 200 1988 291-9
[PubMed: 3373529]
http://dx.doi.org/10.1016/0022-2836(88)90241-0
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Kaminishi T, Wilson DN, Takemoto C, Harms JM, Kawazoe M, Schluenzen F, Hanawa-Suetsugu K, Shirouzu M, Fucini P, Yokoyama S.
A snapshot of the 30S ribosomal subunit capturing mRNA via the Shine-Dalgarno interaction.
Structure 15 2007 289-97
[PubMed: 17355865]
http://dx.doi.org/10.1016/j.str.2006.12.008
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Borovinskaya MA, Shoji S, Fredrick K, Cate JH.
Structural basis for hygromycin B inhibition of protein biosynthesis.
RNA 14 2008 1590-9
[PubMed: 18567815]
http://dx.doi.org/10.1261/rna.1076908
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Bingel-Erlenmeyer R, Kohler R, Kramer G, Sandikci A, Antolic S, Maier T, Schaffitzel C, Wiedmann B, Bukau B, Ban N.
A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing.
Nature 452 2008 108-11
[PubMed: 18288106]
http://dx.doi.org/10.1038/nature06683
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InterPro 23.1
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