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Enzymic methylation of arginyl residues in -gly-arg-gly- peptides.

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dc.contributor.authorHyun, YL-
dc.contributor.authorLew, DB-
dc.contributor.authorPark, SH-
dc.contributor.authorKim, CW-
dc.contributor.authorPaik, WK-
dc.contributor.authorKim, S-
dc.date.accessioned2011-07-27-
dc.date.available2011-07-27-
dc.date.issued2000-
dc.identifier.issn0264-6021-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/3614-
dc.description.abstractN(G)-Methylation of arginine residues in many nucleic-acid-binding proteins are formed post-translationally, catalysed by S-adenosylmethionine:protein-arginine N-methyltransferase in their glycine-rich and arginine-rich motifs. The amino acid sequences of the stimulator of HIV-1 TAR (Tat-responsive element) RNA-binding protein (SRB) and fibronectin also show the presence of the internal -Gly-Arg-Gly- (-GRG-) sequence, which is potentially methylatable by the methyltransferase. To investigate the sequence requirement for methylation of these proteins, several synthetic oligopeptides with different chain lengths and sequences similar to the -GRG- regions of SRB and fibronectin were synthesized. Whereas the heptapeptide AGGRGKG (residues 16-22 in SRB) served as the methyl acceptor for the methyltransferase with a K(m) of 50 microM, the 19-mer peptide (residues 10-28 in SRB) was methylated with a K(m) of 8.3 microM, indicating that a greater peptide chain length yields a better methyl acceptor. Product analysis of the methylated [methyl-(14)C]SRB-peptide by HPLC indicated the formation of N(G)-monomethylarginine and N(G),N(G)-dimethyl(asymmetric)arginine. Synthetic peptides containing the cell attachment sequence [Arg-Gly-Asp ('RGD')] in fibronectin, GRGDSPK, GGRGDSPK and GGGRGDSPK, were also studied; whereas GRGDSPK was a poor methyl acceptor, the longer peptides were better methyl acceptors. To provide an understanding of the effect of methylation on fibronectin peptide, arginine-unmethylated and methylated GGRGDSPK were compared for their effect on the mitogenesis induced by beta-hexosaminidase A and an agonistic antibody (mAb(15)) in bovine tracheal smooth-muscle cells; whereas the former inhibited 35-67% of mitogenesis at a concentration of 5-10 microM, the latter did not block mitogenesis. This lack of inhibition by the insertion of a methyl group on the arginyl residue of the cell attachment sequence might be due to the hindrance of the binding of fibronectin peptide to integrins.-
dc.language.isoen-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHAnimals-
dc.subject.MESHArginine-
dc.subject.MESHCattle-
dc.subject.MESHChromatography, High Pressure Liquid-
dc.subject.MESHChromatography, Ion Exchange-
dc.subject.MESHDNA Replication-
dc.subject.MESHFibronectins-
dc.subject.MESHKinetics-
dc.subject.MESHLiver-
dc.subject.MESHMethylation-
dc.subject.MESHOligopeptides-
dc.subject.MESHProtein-Arginine N-Methyltransferases-
dc.subject.MESHRats-
dc.titleEnzymic methylation of arginyl residues in -gly-arg-gly- peptides.-
dc.typeArticle-
dc.identifier.pmid10839988-
dc.identifier.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221099/-
dc.contributor.affiliatedAuthor백, 운기-
dc.type.localJournal Papers-
dc.citation.titleThe Biochemical journal-
dc.citation.volume348-
dc.citation.numberPt3-
dc.citation.date2000-
dc.citation.startPage573-
dc.citation.endPage578-
dc.identifier.bibliographicCitationThe Biochemical journal, 348(Pt3). : 573-578, 2000-
dc.identifier.eissn1470-8728-
dc.relation.journalidJ002646021-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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