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Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate.
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- Additional Information
- Source:
Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 0404511 Publication Model: Print Cited Medium: Print ISSN: 0036-8075 (Print) Linking ISSN: 00368075 NLM ISO Abbreviation: Science Subsets: MEDLINE
- Publication Information:
Publication: : Washington, DC : American Association for the Advancement of Science
Original Publication: New York, N.Y. : [s.n.] 1880-
- Subject Terms:
- 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.
- Grant Information:
GM12350 United States GM NIGMS NIH HHS; GM1553 United States GM NIGMS NIH HHS; GM19043-16 United States GM NIGMS NIH HHS
- Accession Number:
0 (Bacterial Outer Membrane Proteins)
0 (Bacterial Proteins)
0 (Ion Channels)
0 (Porins)
30KYC7MIAI (Aspartic Acid)
GL19M2KE52 (Triethylenephosphoramide)
- Publication Date:
Date Created: 19890915 Date Completed: 19891013 Latest Revision: 20220318
- Publication Date:
20240829
- Accession Number:
10.1126/science.2476847
- Accession Number:
2476847
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