Post-Translational Methylations of Ribosomal Proteins

Alix, Jean-Hervé

doi:10.1007/978-1-4684-9042-8_30

Cited by 8 publications

(6 citation statements)

References 96 publications

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“…Regulation of protein function by acetylation is one of the major control systems in eukaryotes, but recently this type of control has been identified for some E. coli TFs as well, including McbR, RcsB, RutR, CRP, Rho, and Rsd (68,69). Protein methylation takes place for a number of ribosomal proteins (70). The TF Ada is methylated as an intermediate during its function of removing the methyl group from alkylated DNA (71).…”

Section: Figmentioning

confidence: 99%

Intracellular Concentrations of 65 Species of Transcription Factors with Known Regulatory Functions in Escherichia coli

et al. 2014

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The expression pattern of the Escherichia coli genome is controlled in part by regulating the utilization of a limited number of RNA polymerases among a total of its approximately 4,600 genes. The distribution pattern of RNA polymerase changes from modulation of two types of protein-protein interactions: the interaction of core RNA polymerase with seven species of the sigma subunit for differential promoter recognition and the interaction of RNA polymerase holoenzyme with about 300 different species of transcription factors (TFs) with regulatory functions. We have been involved in the systematic search for the target promoters recognized by each sigma factor and each TF using the newly developed Genomic SELEX system. In parallel, we developed the promoter-specific (PS)-TF screening system for identification of the whole set of TFs involved in regulation of each promoter. Understanding the regulation of genome transcription also requires knowing the intracellular concentrations of the sigma subunits and TFs under various growth conditions. This report describes the intracellular levels of 65 species of TF with known function in E. coli K-12 W3110 at various phases of cell growth and at various temperatures. The list of intracellular concentrations of the sigma factors and TFs provides a community resource for understanding the transcription regulation of E. coli under various stressful conditions in nature.

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Section: Figmentioning

confidence: 99%

Intracellular Concentrations of 65 Species of Transcription Factors with Known Regulatory Functions in Escherichia coli

et al. 2014

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“…Importantly, some of the methylated proteins have important functions in translation, as for example, L7/L12 of E. coli , which is essential for translation accuracy; L11, which belongs to the GTPase‐associated centre of the 50S ribosomal subunit (Agrawal et al ., 2001; Li et al ., 2006); and L3, which is involved in assembly (Lhoest and Colson, 1977). Furthermore, E. coli L11 and yeast L12 and rat L12, which can be considered as functional homologues, are all methylated (Alix et al ., 1979a; Jerez and Weissbach, 1980; Alix, 1988) and contain N ‐ε‐TML (Chang et al ., 1974; Lhoest et al ., 1984). Methylation of E. coli L11 may play an important role in protein interactions with 23S rRNA, other RPs or TFs (Chang et al ., 1974; Dognin and Wittmann‐Liebold, 1977; 1980a; Alix et al ., 1979b; Agrawal et al ., 2001), and in assembly of L16 into the 50S (Rohl and Nierhaus, 1979; Nierhaus and Lafontaine, 2004).…”

Section: Methylated Rps and Known Methylated Sites And Residuesmentioning

confidence: 99%

Methylation of proteins involved in translation

Polevoda¹,

Sherman²

2007

Molecular Microbiology

126

111

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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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“…However, some residual Lii methyltransferase activity can be detected in extracts from strains carrying prmAl orprmA3 mutations (2,15). This residual activity could account for the lack of a phenotype associated with the prmA mutations.…”

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confidence: 99%

“…Posttranslational modification of several ribosomal proteins is a general phenomenon observed in both prokaryotes and eukaryotes (2). Although much information on the expression of the genes for bacterial rRNAs and ribosomal proteins is available (29), little attention has been given to their posttranslational modifications, which are actually quite numerous.…”

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“…In vitro methylation experiments with ribosomes from the prmA strains and with extracts from prmA+ bacteria and radioactively labeled S-adenosyl-L-methionine show that the prmA mutations result in loss of methyl groups from both the N-terminal alanine and the internal lysine residues (5,14,15). However, some residual Lii methyltransferase activity can be detected in extracts from strains carrying prmAl orprmA3 mutations (2,15). This residual activity could account for the lack of a phenotype associated with the prmA mutations.…”

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Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12

1993

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Genetic complementation and enzyme assays have shown that the DNA region between panF, which encodes pantothenate permease, and orfl, the first gene of thefis operon, encodes prmA, the genetic determinant for the ribosomal protein Lll methyltransferase. Sequencing of this region identified one long open reading frame that encodes a protein of 31,830 Da and corresponds to the prmA gene. We found, both in vivo and in vitro, that prmA is expressed from promoters located upstream ofpanF and thus that the panF and prmA genes constitute a bifunctional operon. We located the major 3' end ofprmA transcripts 90 nucleotides downstream of the stop codon of prmA in the DNA region upstream of the fis operon, a region implicated in the control of the expression of thefis operon. Although no promoter activity was detected immediately upstream of prmA, Si mapping detected 5' ends of mRNA in this region, implying that some mRNA processing occurs within the bicistronic panF-prmA mRNA.Posttranslational modification of several ribosomal proteins is a general phenomenon observed in both prokaryotes and eukaryotes (2). Although much information on the expression of the genes for bacterial rRNAs and ribosomal proteins is available (29), little attention has been given to their posttranslational modifications, which are actually quite numerous. In Escherichia coli, proteins such as S5, S18, L12, and EF-Tu are acetylated at their N-terminal residues (L7 is the acetylated form of L12). Others modifications include addition of amino acids to the polypeptide chain, e.g., addition of one to four glutamic acid residues to the C terminal of ribosomal protein S6 (25,30). However, the most frequent modification is methylation. Several ribosomal proteins, e.g., Sli, L3, L7/L12, Lii, L16, and L33, as well as EF-Tu and IF3, have Nmethylated amino acids at specific positions (reviewed in reference 2). Lii is the most heavily methylated ribosomal protein, with three trimethylated amino acid residues: two Ns-trimethyllysines at positions 3 and 39 (19) and an aminoterminal 35). Methylation of ribosomal protein L 1I requires S-adenosyl-L-methionine as a methyl group donor (4) in a co-or posttranslational event.Mutations show that the prmA mutations result in loss of methyl groups from both the N-terminal alanine and the internal lysine residues (5, 14, 15). However, some residual Lii methyltransferase activity can be detected in extracts from strains carrying prmAl orprmA3 mutations (2,15). This residual activity could account for the lack of a phenotype associated with the prmA mutations. Since single mutations apparently result in the absence of both internal and N-terminal methyl groups from Li 1, it seems possible that the same enzyme is responsible for the methylation of all three amino acids. If this is the case, then the distinctive trimethylation of two different amino acids at three different loci when all of the other lysine residues of the protein are unmodified poses an interesting problem of enzyme specificity. We cannot, however, rule ou...

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Post-Translational Methylations of Ribosomal Proteins

Cited by 8 publications

References 96 publications

Intracellular Concentrations of 65 Species of Transcription Factors with Known Regulatory Functions in Escherichia coli

Intracellular Concentrations of 65 Species of Transcription Factors with Known Regulatory Functions in Escherichia coli

Methylation of proteins involved in translation

Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12

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