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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 ribosomic proteins have been isolated and specific anti-bodies 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. A representation of the 3D structure of myoglobin, showing coloured alpha helices. ...
A non-coding RNA (ncRNA) is any RNA molecule that functions without being translated into a protein. ...
Translation is the second process of protein biosynthesis (part of the overall process of gene expression). ...
Binomial name Escherichia coli T. Escherich, 1885 Low-temperature electron micrograph of a cluster of E. coli bacteria, magnified 10,000 times. ...
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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.
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
- De Robertis and De Robertis, Biología Celular y Molecular 10th ed., El Ateneo, Buenos Aires, 1982, ISBN 950-02-0027-9 (in Spanish)
1982 (MCMLXXXII) was a common year starting on Friday of the Gregorian calendar. ...
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