Identification of Methylated Amino Acids During Sequence Analysis. Application to the<i>Escherichia coli</i>Ribosomal Protein L11

Dognin, Mai J.; Wittmann‐Liebold, Brigitte

doi:10.1515/bchm2.1980.361.2.1697

Cited by 15 publications

(3 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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). On the other hand, only secondary‐ or late‐assembly RPs of the small ribosomal subunit are known to be methylated in bacteria, i.e.…”

Section: Methylated Rps and Known Methylated Sites And Residuesmentioning

confidence: 99%

Methylation of proteins involved in translation

Polevoda¹,

Sherman²

2007

Molecular Microbiology

129

110

View full text Add to dashboard Cite

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.

show abstract

Section: Methylated Rps and Known Methylated Sites And Residuesmentioning

confidence: 99%

Methylation of proteins involved in translation

Polevoda¹,

Sherman²

2007

Molecular Microbiology

129

110

View full text Add to dashboard Cite

show abstract

“…Yeast Rpl12ab and its bacterial ortholog L11 are methylated N-terminally and human Rpl12 is also predicted to be methylated at the N-terminus (Dognin and Wittmann-Liebold 1980;Webb et al 2010b). In E. coli, L3 is methylated on a glutamine residue that aligns close to the methylated histidine site on Rpl3 in S. cerevisiae (Muranova et al 1978;Webb et al 2010a).…”

Section: Introductionmentioning

confidence: 99%

Methylation of yeast ribosomal protein Rpl3 promotes translational elongation fidelity

Al-Hadid

Roy

Chanfreau

et al. 2016

RNA

View full text Add to dashboard Cite

Rpl3, a highly conserved ribosomal protein, is methylated at histidine 243 by the Hpm1 methyltransferase in Saccharomyces cerevisiae. Histidine 243 lies close to the peptidyl transferase center in a functionally important region of Rpl3 designated as the basic thumb that coordinates the decoding, peptidyl transfer, and translocation steps of translation elongation. Hpm1 was recently implicated in ribosome biogenesis and translation. However, the biological role of methylation of its Rpl3 substrate has not been identified. Here we interrogate the role of Rpl3 methylation at H243 by investigating the functional impact of mutating this histidine residue to alanine (rpl3-H243A). Akin to Hpm1-deficient cells, rpl3-H243A cells accumulate 35S and 23S pre-rRNA precursors to a similar extent, confirming an important role for histidine methylation in pre-rRNA processing. In contrast, Hpm1-deficient cells but not rpl3-H243A mutants show perturbed levels of ribosomal subunits. We show that Hpm1 has multiple substrates in different subcellular fractions, suggesting that methylation of proteins other than Rpl3 may be important for controlling ribosomal subunit levels. Finally, translational fidelity assays demonstrate that like Hpm1-deficient cells, rpl3-H243A mutants have defects in translation elongation resulting in decreased translational accuracy. These data suggest that Rpl3 methylation at H243 is playing a significant role in translation elongation, likely via the basic thumb, but has little impact on ribosomal subunit levels. Hpm1 is therefore a multifunctional methyltransferase with independent roles in ribosome biogenesis and translation.

show abstract

“…Several ribosomal proteins, e.g., Sli, L3, L7/L12, Lii, L16, and L33, as well as EF-Tu and IF3, have N-methylated 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 Nox-trimethylalanine (18,35). Methylation of ribosomal protein L 1I requires S-adenosyl-L-methionine as a methyl group donor (4) in a co-or posttranslational event.…”

mentioning

confidence: 99%

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

1993

View full text Add to dashboard Cite

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...

show abstract

Identification of Methylated Amino Acids During Sequence Analysis. Application to theEscherichia coliRibosomal Protein L11

Cited by 15 publications

References 15 publications

Methylation of proteins involved in translation

Methylation of proteins involved in translation

Methylation of yeast ribosomal protein Rpl3 promotes translational elongation fidelity

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

Contact Info

Product

Resources

About