Literature DB >> 118166

In vivo methylation of elongation factor Tu of Escherichia coli.

M Ohba, O Koiwai, S Tanada, H Hayashi.   

Abstract

A protein existing mainly in the supernatant fraction of Escherichia coli was found to be methylated by accepting the methyl moiety originating from methionine. The protein was identified as peptide synthesis elongation factor Tu (EF-Tu) by the following criteria. 1) The methylatable protein separated at the same position as purified EF-Tu on two-dimensional gel electrophoresis. 2) The methylatable protein interacted with antiserum specific for EF-Tu. Amino acid analysis of the methyl-labeled protein suggested that the site of methylation was an epsilon-amino group of lysine.

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Year:  1979        PMID: 118166     DOI: 10.1093/oxfordjournals.jbchem.a132638

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  Chimeric chemosensory transducers of Escherichia coli.

Authors:  A Krikos; M P Conley; A Boyd; H C Berg; M I Simon
Journal:  Proc Natl Acad Sci U S A       Date:  1985-03       Impact factor: 11.205

2.  Demethylation of methyl-accepting chemotaxis proteins in Escherichia coli induced by the repellents glycerol and ethylene glycol.

Authors:  K Oosawa; Y Imae
Journal:  J Bacteriol       Date:  1984-02       Impact factor: 3.490

  2 in total

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