Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate

Ryutaro Utsumi, Renee E. Brissette, Arfaan Rampersaud, Steven A. Forst, Kenji Oosawa, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

181 Scopus citations

Abstract

The Tar chemoreceptor of Escherichia coli is a membrane-bound sensory protein that facilitates bacterial chemotaxis in response to aspartate. The EnvZ molecule has a membrane topology similar to Tar and is a putative osmosensor that is required for osmoregulation of the genes for the major outer membrane porin proteins, OmpF and OmpC. The cytoplasmic signaling domain of Tar was replaced with the carboxyl portion of EnvZ, and the resulting chimeric receptor activated transcription of the ompC gene in response to aspartate. The activation of ompC by the chimeric receptor was absolutely dependent on OmpR, a transcriptional activator for ompF and ompC.

Original languageEnglish (US)
Pages (from-to)1246-1249
Number of pages4
JournalScience
Volume245
Issue number4923
DOIs
StatePublished - 1989

All Science Journal Classification (ASJC) codes

  • General

Fingerprint

Dive into the research topics of 'Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate'. Together they form a unique fingerprint.

Cite this