Methylgroups of ribosomal protein L11 are not related to the synthesis of ppGpp

Röhl, Roland; Nierhaus, Knud H.

doi:10.1007/bf00337795

Cited by 5 publications

(3 citation statements)

References 20 publications

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“…L11 Lys39 on the surface of helix α2 is oriented toward the ribosome surface in a position that is unlikely to interact with either elongation or release factors, whereas Lys3 is positioned such that methylation of this residue could potentially influence interaction with EF‐G. L11 methylation does not influence the stringent response (Rohl and Nierhaus, 1979), although there are other GTPases that interact with the ribosome, and probably with L11 directly, including members of the Obg family of GTPases, which participate in a variety of cellular response pathways (Kukimoto‐Niino et al , 2004).…”

Section: Discussionmentioning

confidence: 99%

Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA

DeMi̇rci̇

Gregory

Dahĺberg

et al. 2007

EMBO J

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Bacterial ribosomal protein L11 is post-translationally trimethylated at multiple residues by a single methyltransferase, PrmA. Here, we describe four structures of PrmA from the extreme thermophile Thermus thermophilus. Two apo-PrmA structures at 1.59 and 2.3 Å resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 Å each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions. The fourth structure, the PrmA-L11 enzyme-substrate complex at 2.4 Å resolution, illustrates the highly specific interaction of the N-terminal domain with its substrate and places Lys39 in the PrmA active site. The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitating the dissociation of PrmA from L11. Finally, the mode of interaction of PrmA with L11 explains its observed preference for L11 as substrate before its assembly into the 50S ribosomal subunit.

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Section: Discussionmentioning

confidence: 99%

Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA

DeMi̇rci̇

Gregory

Dahĺberg

et al. 2007

EMBO J

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“…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

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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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“…After centrifugation (2 min; I centrifuge, model 3200), 5 of the supern spotted on polyethylenimine thin-layer grams. Chromatography using KH2PO4 (0 3.4) was followed by autoradiography to det actively labeled nucleotides (11,15). Mini incubated for a total of6 h, and the leftmost in the figure show the nucleotides preseni fected minicells sampled at each hour of in The rightmost six tracks show the nucleotid sized in minicells infected at each hour by be seen that ppGpp and pppGpp do not a( in uninfected minicells, but are synthesiz sponse to T7 infection.…”

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confidence: 99%