Selection of ion channel elements in the serine and aspartate methyl-accepting chemotaxis proteins of bacteria

Edward M. Kosower*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Two plausible, transmembrane ion channel elements (These 'elements' are α-helical sequences of 24 amino acids in which polar, hydrophilic side chains occupy one side and hydrophobic side chains the other) have been identified in the serine chemoreceptor-methyl-accepting chemotaxis protein (MCP)(SerR) of E. coli and the aspartate chemoreceptor-MCP (AspR) of S. typhimurium. That the chemoreceptor might serve as, or activate, an ion channel is supported strongly by the occurrence of membrane depolarization, specific peptide methylation and neurotoxin inhibition of response in the chemotaxis of S. aurantiaE.P. Greenberg, refs. 13-18.

Original languageEnglish
Pages (from-to)648-652
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume115
Issue number2
DOIs
StatePublished - 15 Sep 1983

Fingerprint

Dive into the research topics of 'Selection of ion channel elements in the serine and aspartate methyl-accepting chemotaxis proteins of bacteria'. Together they form a unique fingerprint.

Cite this