The primary structure of L11, the most heavily methylated protein from <i>Escherichia coli</i> ribosomes

Dognin, Mai J.; Wittmann‐Liebold, Brigitte

doi:10.1016/0014-5793(77)80721-7

Cited by 58 publications

(29 citation statements)

References 44 publications

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“…L16 and L11 were treated with reagent as described in Table 1 photoinactivation of L6 results in reduced stimulation of L16-mediated transesterification but L1 I-induced stimulation was insensitive to such treatments ( Table 1). The partial inhibition in the case of L6 suggests that histidine in L6 may contribute some functional role and the insensitivity of L11 was obviously due to the lack of a histidine residue [33]. Dip-F (Table I), however, markedly affected the L11 stimulation of transesterification, which implies that -Ser-Phe-residues play an important role as suggested earlier.…”

Section: Resultsmentioning

confidence: 56%

“…L6 contains two histidine residues, at least one HisLys, several serines but only one -Ser-Phe-. In L11 [33] and L16 [32] this combination is located near the N-terminal portion of these proteins. Ethoxyformylation or pyridoxal phosphate The samples (100 pl) were withdrawn at indicated intervals and assayed for transesterification as described in Materials and Methods.…”

Section: Resultsmentioning

confidence: 99%

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L16, a bifunctional ribosomal protein and the enhancing effect of L6 and L11

Baxter

Zahid

1986

European Journal of Biochemistry

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L16 exhibits both peptide bond and transesterification activities when reconstituted into 2 M LiCl core particles. L6 and L11, when reconstituted in a similar manner in the absence of L16, manifest significant transesterification activity. Both L6 and L11 enhance the transesterification activity of L16; L11 being more active than L6 in this respect. However, both L6 and L11 have minimal effect on peptide bond formation when reconstituted with L16 at concentrations more than 2.5 M equivalents. Both L6 and L11 exhibit a differential effect on transesterification.The affinity-labelling agents, like PhCH2S02F, diisopropylfluorophosphate and ethoxyformic anhydride, have been used to explore the role of residues in peptide bond formation and transesterification. It is proposed that the Ser-Phe combination present in L16, L11 and L6 is involved in transesterification in addition to the single histidine in L16. The single histidine in L16 appears to be important in the catalysis of peptide bond formation and transesterification.Peptidyltransferase is a central enzyme on the large (50s) ribosomal subunits, which catalyses peptide bond formation [l, 21 and also may be involved in peptide chain termination Experimental approaches, involving partial reconstitution[5], affinity labelling or chemical modifications [6] , mutants [7, 81 and immunological techniques [9], have been used in attempts to delineate the role of the ribosomal proteins essential for peptide bond formation of peptide chain termination. Partial reconstitution studies indicate that L16, which is completely split off the 50s particles by 1.5 M LiCl, is the only protein which restores activity when added back to the depleted core particles at 2.5 molar excess or higher concentration [lo]. L16 appears to be most active protein involved in many catalytic functions of peptidyltransferase [ll]. It is interesting to note that to date Escherichiu coli mutants lacking L16 have not been reported [ll].L6 and L11 are two other proteins which have been shown to exert a stimulatory effect on L16-mediated peptidyltransferase activity. L6 forms a specific complex with 23s RNA [12] and is considered to be located at the aminoacyl-tRNAbinding site of the peptidyltransferase centre [13] whereas L11 has been implicated as part of the domain surrounding the peptidyltransferase centre [lo]. Using an Lll-deficient mutant, L11 has been shown to have little effect on peptidyltransferase activity [7, 81. Antibodies specific to L16 and L11 affected the peptidyl-tRNA hydrolysis and, therefore, were considered to be involved in peptide chain termination [ 141. However, peptidyltransferase and peptide chain termination were little affected in L11-depleted reconstituted particles [15]. The specific role of L11 has recently 13~41.

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Section: Resultsmentioning

confidence: 56%

Section: Resultsmentioning

confidence: 99%

L16, a bifunctional ribosomal protein and the enhancing effect of L6 and L11

Baxter

Zahid

1986

European Journal of Biochemistry

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“…Escherichia coli L11, one of the most well characterized ribosomal proteins, is ␣-N-trimethylated at Ala 1 and ⑀-N-trimethylated at Lys 3 and Lys 39 (10). These methyl groups are added by a single methyltransferase called PrmA (11).…”

mentioning

confidence: 99%

“…Rpl23 is specifically ⑀-N-dimethylated at two residues, Lys 105 and Lys 109 , and these modifications are catalyzed by the SET domain-containing methyltransferase Rkm1 (15,16). S. cerevisiae Rpl12, the counterpart of bacterial L11, is also modified,: by ⑀-N-dimethylated at Lys 3 , ⑀-N-trimethylation at Lys 10 , and ␦-N-monomethylation at Arg 66 (17,18). Rkm2, another SET domain-containing protein, and Rmt2, a protein arginine methyltransferase, catalyze the methylation at Lys 10 and Arg 66 of Rpl12, respectively (17,18).…”

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confidence: 99%

A Conserved SET Domain Methyltransferase, Set11, Modifies Ribosomal Protein Rpl12 in Fission Yeast

Sadaie

Shinmyozu²,

Nakayama

2008

Journal of Biological Chemistry

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SET domain-containing methyltransferases post-translationally modify a variety of cellular proteins, such as histones, cytochrome c, ribulose-bisphosphate carboxylase/oxygenase, and ribosomal proteins. In the fission yeast Schizosaccharomyces pombe, at least 13 SET domain-containing proteins have been identified in the genome, four of which are involved in transcriptional regulation through their modification of histone tails. However, the roles played by the other SET domain proteins in cellular processes and their physiological substrates remain unresolved. We show here that S. pombe Set11, a SET domaincontaining protein encoded by SPCC1223.04c, specifically modifies Rpl12 (ribosomal protein L12). Recombinant Set11 prepared from Escherichia coli had catalytic activity and methylated a 17-kDa polypeptide in cellular extracts of set11 mutant cells. The methylated protein was isolated by two-dimensional gel electrophoresis or by reverse-phase chromatography and was identified as Rpl12 by mass spectrometry. In vitro methylation experiments using wild-type and mutant Rpl12 proteins verified that Set11 modified recombinant Rpl12 and suggested that its potential target site was lysine 3. The methylation site modified by Set11 was also confirmed by mass spectrometric analysis, which also revealed other unique methylation sites of Rpl12. Finally, we found that Set11 predominantly localized to the nucleolus and that the overproduction of Set11 caused a severe growth defect. These results suggest that Rpl12 methylation occurs during the ribosomal assembly processes and that control of the Set11 expression level is important for its cellular function.

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“…18–20 The placement of these modified residues on the parent structure was performed by comparing the putative sequence of 1 to that of 4 . Upon reexamination of our NMR data, every correlation from 2D-NMR matched the predicted structure, while we did not find a single correlation that violated the proposed structure (Fig.…”

Section: Resultsmentioning

confidence: 99%

Accessing chemical diversity from the uncultivated symbionts of small marine animals

et al. 2018

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Chemistry drives many biological interactions between the microbiota and host animals, yet it is often challenging to identify the chemicals involved. This poses a problem, as such small molecules are excellent sources of potential pharmaceuticals, pretested by nature for animal compatibility. We discovered anti-HIV compounds from small, marine tunicates from the Eastern Fields of Papua New Guinea. Tunicates are a reservoir for novel bioactive chemicals, yet their small size often impedes identification or even detection of the chemicals within. We solved this problem by combining chemistry, metagenomics, and synthetic biology to directly identify and synthesize the natural products. We show that these anti-HIV compounds, the divamides, are a novel family of lanthipeptides produced by symbiotic bacteria living in the tunicate. Neighboring animal colonies contain structurally related divamides that differ starkly in their biological properties, suggesting a role for biosynthetic plasticity in a native context where biological interactions take place.

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The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes

Cited by 58 publications

References 44 publications

L16, a bifunctional ribosomal protein and the enhancing effect of L6 and L11

L16, a bifunctional ribosomal protein and the enhancing effect of L6 and L11

A Conserved SET Domain Methyltransferase, Set11, Modifies Ribosomal Protein Rpl12 in Fission Yeast

Accessing chemical diversity from the uncultivated symbionts of small marine animals

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