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PMID: 3297352 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Additive and independent responses in a single receptor: aspartate and maltose stimuli on the tar protein.

Cell ·Vol. 50 ·No. 2 ·1987-07-17 ·Pages 171-80

Mowbray SL, Koshland DE

Abstract

The aspartate and maltose responses of E. coli are mediated through a single membrane receptor, yet the responses are independent and additive. Both stimuli cause methylation of the same 4 glutamic acid residues. More extensive methylation occurs when a cell that has adapted to one stimulus is exposed to the second, or when both stimuli are added simultaneously. The degree of methylation, as well as receptor migration on two-dimensional gels, demonstrates that only one type of protein is involved, rather than two different receptors arising from differential processing of a single gene. A conformational "push-pull" mechanism in which binding of stimulus and covalent modification, producing opposing stresses, can explain these diverse results.

MeSH Terms
ATP-Binding Cassette Transporters Aspartic Acid/pharmacology Bacterial Proteins/metabolism Carrier Proteins/genetics,metabolism Escherichia coli/drug effects,genetics,metabolism Escherichia coli Proteins Genes Genes, Bacterial Maltose/metabolism,pharmacology Maltose-Binding Proteins Methylation Models, Biological Monosaccharide Transport Proteins Mutation Plasmids
Chemicals
ATP-Binding Cassette Transporters Bacterial Proteins Carrier Proteins Escherichia coli Proteins Maltose-Binding Proteins Monosaccharide Transport Proteins maltose transport system, E coli Aspartic Acid Maltose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mowbray S L
Koshland D E
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
1987-07-17
Pages
171-80
Language
English
Region
United States
NLM ID
0413066
Subset
IM
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