EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is phosphorylated in vitro.

M. M. Igo, T. J. Silhavy

Research output: Contribution to journalArticle

104 Scopus citations

Abstract

By fusing the transcriptional and translational start signals of lacZ to envZ, we have obtained high-level synthesis of a truncated EnvZ protein (EnvZ115) in which the first 38 amino acids of EnvZ are replaced with the first 8 amino acids of LacZ. Using this construct, we have partially purified the EnvZ115 protein and demonstrated that this protein can be phosphorylated in vitro. We suggest that phosphorylation may be an important feature of EnvZ function.

Original languageEnglish (US)
Pages (from-to)5971-5973
Number of pages3
JournalJournal of bacteriology
Volume170
Issue number12
DOIs
StatePublished - Dec 1988

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Microbiology

Fingerprint Dive into the research topics of 'EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is phosphorylated in vitro.'. Together they form a unique fingerprint.

  • Cite this