Document Detail

Hydrogen exchange reveals a stable and expandable core within the aspartate receptor cytoplasmic domain.
MedLine Citation:
PMID:  11553619     Owner:  NLM     Status:  MEDLINE    
Intensive study of bacterial chemoreceptors has not yet revealed how receptor methylation and ligand binding alter the interactions between the receptor cytoplasmic domain and the CheA kinase to control kinase activity. Both monomeric and dimeric forms of an Asp receptor cytoplasmic fragment have been shown to be highly dynamic, with a small core of slowly exchanging amide hydrogens (Seeley, S. K., Weis, R. M., and Thompson, L. K. (1996) Biochemistry 35, 5199-5206). Hydrogen exchange studies of the wild-type cytoplasmic fragment and an S461L mutant thought to mimic the kinase-inactivating state are used to investigate the relationship between the stable core and dimer dissociation. Our results establish that (i) decreasing pH stabilizes the dimeric state, (ii) the stable core is present also in the transition state for dissociation, and (iii) this core is expanded significantly by small changes in electrostatic and hydrophobic interactions. These kinase-inactivating changes stabilize both the monomeric and the dimeric states of the protein, which has interesting implications for the mechanism of kinase activation. We conclude that the cytoplasmic domain is a flexible region poised for stabilization by small changes in electrostatic and hydrophobic interactions such as those caused by methylation of glutamate residues and by ligand-induced conformational changes during signaling.
O J Murphy; X Yi; R M Weis; L K Thompson
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Publication Detail:
Type:  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.     Date:  2001-09-11
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  276     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-11-12     Completed Date:  2001-12-26     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  43262-9     Citation Subset:  IM    
Graduate Program in Molecular and Cellular Biology, and the Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003-4510, USA.
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MeSH Terms
Chromatography, Gel
Cytoplasm / chemistry*
Glutamic Acid / chemistry
Histidine / chemistry
Hot Temperature
Hydrogen / chemistry,  metabolism*
Hydrogen-Ion Concentration
Models, Chemical
Models, Molecular
Plasmids / metabolism
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Receptors, Amino Acid / chemistry*
Time Factors
Tritium / chemistry
Grant Support
Reg. No./Substance:
0/Ligands; 0/Receptors, Amino Acid; 0/aspartic acid receptor; 10028-17-8/Tritium; 1333-74-0/Hydrogen; 56-86-0/Glutamic Acid; 71-00-1/Histidine

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