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Title: Site-directed cross-linking: establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis

Abstract

Cysteine residues introduced at specific locations in the aspartate receptor of Salmonella typhimurium provide anchor points for cross-linking and serve as chemical markers for structural studies of this oligomeric receptor. These markers have been used to measure the rate of subunit exchange between oligomeric receptors and to show that ligand binding inhibits this exchange. The cysteine-containing receptors can be oxidatively cross-linked to completion within the oligomeric receptor, indicating that the receptor has an even number of subunits. Based on this observation, a technique has been developed that can be used to determine the oligomeric structure of proteins under a variety of experimental conditions. The technique involves the measurement of the effect of dilution by cysteineless receptor subunits on cross-linking and reveals that the aspartate receptor is dimeric in detergent solution, in a mixed-micelle system, and in reconstituted membrane vesicles. Binding of aspartate does not change the oligomeric structure of the receptor, indicating that transmembrane signaling occurs within an oligomeric receptor of constant size.

Authors:
;
Publication Date:
Research Org.:
Univ. of California, Berkeley (USA)
OSTI Identifier:
6838150
Resource Type:
Journal Article
Journal Name:
J. Biol. Chem.; (United States)
Additional Journal Information:
Journal Volume: 263:13
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PROTEINS; BIOCHEMISTRY; RECEPTORS; CROSS-LINKING; ASPARTIC ACID; CYSTEINE; HEAVY WATER; OXYGEN 18; SALMONELLA TYPHIMURIUM; TRITIUM COMPOUNDS; AMINO ACIDS; BACTERIA; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; CHEMISTRY; EVEN-EVEN NUCLEI; HYDROGEN COMPOUNDS; ISOTOPES; LABELLED COMPOUNDS; LIGHT NUCLEI; MEMBRANE PROTEINS; MICROORGANISMS; NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; OXYGEN COMPOUNDS; OXYGEN ISOTOPES; POLYMERIZATION; SALMONELLA; STABLE ISOTOPES; THIOLS; WATER; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Milligan, D L, and Koshland, Jr, D E. Site-directed cross-linking: establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. United States: N. p., 1988. Web.
Milligan, D L, & Koshland, Jr, D E. Site-directed cross-linking: establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. United States.
Milligan, D L, and Koshland, Jr, D E. 1988. "Site-directed cross-linking: establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis". United States.
@article{osti_6838150,
title = {Site-directed cross-linking: establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis},
author = {Milligan, D L and Koshland, Jr, D E},
abstractNote = {Cysteine residues introduced at specific locations in the aspartate receptor of Salmonella typhimurium provide anchor points for cross-linking and serve as chemical markers for structural studies of this oligomeric receptor. These markers have been used to measure the rate of subunit exchange between oligomeric receptors and to show that ligand binding inhibits this exchange. The cysteine-containing receptors can be oxidatively cross-linked to completion within the oligomeric receptor, indicating that the receptor has an even number of subunits. Based on this observation, a technique has been developed that can be used to determine the oligomeric structure of proteins under a variety of experimental conditions. The technique involves the measurement of the effect of dilution by cysteineless receptor subunits on cross-linking and reveals that the aspartate receptor is dimeric in detergent solution, in a mixed-micelle system, and in reconstituted membrane vesicles. Binding of aspartate does not change the oligomeric structure of the receptor, indicating that transmembrane signaling occurs within an oligomeric receptor of constant size.},
doi = {},
url = {https://www.osti.gov/biblio/6838150}, journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 263:13,
place = {United States},
year = {Thu May 05 00:00:00 EDT 1988},
month = {Thu May 05 00:00:00 EDT 1988}
}