Isopeptide linkage between N-alpha-monomethylalanine and lysine in ribosomal protein S11 from Escherichia coli.

А number of ribosomal proteins inEscherichia coliundergo posttranslational modifications. Six ribosomal proteins are methylated (S11, L3, L11, L7/L12, L16, and L33), three proteins are acetylated (S5, S18, and L7), and protein S12 is methylthiolated. Extra amino acid residues are added to protein S6. С-terminal amino acid residues are partially removed from protein L31. The functional significance of these modifications has remained unclear. These modifications are not vital to the cells, and it is likely that they have regulatory functions. This paper reviews all the known posttranslational modifications of ribosomal proteins inEscherichia coli. Certain enzymes responsible for the modifications and mechanisms of enzymatic reactions are also discussed.

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“… Structure of the N-terminal amino acid residue of S11, which is methylated and forms isopeptide linkage [ 25 ]. …”

Section: Methylation Of Ribosomal Proteinsmentioning

confidence: 99%

“…During this process, the peptide bond between the first and second residues (alanine and lysine) in the S11 molecule is destroyed ( Fig. 3 ) [ 25 ].…”

Section: Methylation Of Ribosomal Proteinsmentioning

confidence: 99%

Posttranslational Modifications of Ribosomal Proteins in Escherichia coli

2011

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“…In addition to methylation or acetylation alone, more complex protein modifications were found within RPs S11 and S12, and TF eEF2 (eEF2 modifications described in the next section). For example, besides methylation of the N‐terminal Ala, the formation of an isopeptide bond between Me‐Ala and the ε‐amino group of the subsequent Lys residue was observed (Chen and Chen‐Schmeisser, 1977). Therefore, two amino acids were seen when the N‐terminus of the protein was determined.…”

Section: Methylated Rps and Known Methylated Sites And Residuesmentioning

confidence: 99%

Methylation of proteins involved in translation

Polevoda¹,

Sherman²

2007

Molecular Microbiology

129

110

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SummaryMethylation is one of the most common protein modifications. Many different prokaryotic and eukaryotic proteins are methylated, including proteins involved in translation, including ribosomal proteins (RPs) and translation factors (TFs). Positions of the methylated residues in six Escherichia coli RPs and two Saccharomyces cerevisiae RPs have been determined. At least two RPs, L3 and L12, are methylated in both organisms. Both prokaryotic and eukaryotic elongation TFs (EF1A) are methylated at lysine residues, while both release factors are methylated at glutamine residues. The enzymes catalysing methylation reactions, protein methyltransferases (MTases), generally use S-adenosylmethionine as the methyl donor to add one to three methyl groups that, in case of arginine, can be asymetrically positioned. The biological significance of RP and TF methylation is poorly understood, and deletions of the MTase genes usually do not cause major phenotypes. Apparently methylation modulates intra-or intermolecular interactions of the target proteins or affects their affinity for RNA, and, thus, influences various cell processes, including transcriptional regulation, RNA processing, ribosome assembly, translation accuracy, protein nuclear trafficking and metabolism, and cellular signalling. Differential methylation of specific RPs and TFs in a number of organisms at different physiological states indicates that this modification may play a regulatory role.

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Post-Translational Methylations of Ribosomal Proteins

Alix

1988

Advances in Post-Translational Modifications of Proteins and Aging

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Isopeptide linkage between N-alpha-monomethylalanine and lysine in ribosomal protein S11 from Escherichia coli.

Cited by 9 publications

References 24 publications

Posttranslational Modifications of Ribosomal Proteins in Escherichia coli

Posttranslational Modifications of Ribosomal Proteins in Escherichia coli

Methylation of proteins involved in translation

Post-Translational Methylations of Ribosomal Proteins

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