INVIVO METHYLATION OF ELONGATION FACTOR-TU OF ESCHERICHIA-COLI

被引:9
作者
OHBA, M
KOIWAI, O
TANADA, S
HAYASHI, H
机构
[1] Institute of Molecular Biology, Faculty of Science, Nagoya University, Nagoya, Aichi 464, Chikusa-ku
关键词
D O I
10.1093/oxfordjournals.jbchem.a132638
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 s-amino group of lysine. © 1979, by the Japanese Biochemical Society.
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页码:1233 / 1238
页数:6
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