Identification of a sulfhydryl-reducing agent-inducible protein highly homologous to protein synthesis elongation factor Tu in Bacillus subtilis

T. Wang, H. Kadokura, K. Yada, M. Yamasaki

Research output: Contribution to journalArticle

Abstract

It was examined that the effect of beta-mercaptoethanol and dithiothreitol treatments, which should affect disulfide bond formation of proteins, on cellular protein components of Bacillus subtilis. In LB medium, the treatments induced the synthesis of a 50 kD protein (P50), which is synthesized constitutively under normal growth condition and is a major cytoplasmic protein. P50 was also induced by heat shock, but not by sporulation. In Schaeffer's sporulation medium, however, P50 was not induced by the sulfhydryl-reducing agents. This suggests that the sulfhydryl-reducing agent-inducibility of P50 might depent on specific physiological condition(s). The amino terminal sequences of two of the four main V8 protease fragments of P50 were determined. A search in databases revealed that P50 was highly homologous to protein synthesis elongation factor Tu of B. subtilis.

Original languageEnglish
Pages (from-to)6-12
Number of pages7
JournalWei sheng wu xue bao = Acta microbiologica Sinica
Volume38
Issue number1
Publication statusPublished - 1998 Feb
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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