Document Detail


GTP-yeast actin.
MedLine Citation:
PMID:  12191996     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Because of the apparently greater conformational flexibility of yeast versus muscle actin and the ability of other members in the actin protein superfamily to efficiently use both ATP and GTP, we assessed the ability of yeast actin to function with GTP. Etheno-ATP exchange studies showed that the binding of GTP to yeast actin is about 1/9 as tight as that of ATP in contrast to the 1/1,240 ratio for muscle actin. Proteolysis of GTP-bound G-yeast actin suggests that the conformation of subdomain 2 is very much like that of ATP-bound actin, but CD studies show that GTP-bound actin is less thermostable than ATP-bound actin. GTP-actin polymerizes with an apparent critical concentration of 1.5 microm, higher than that of ATP-actin (0.3 microm) although filament structures observed by electron microscopy were similar. Yeast actin hydrolyzes GTP in a polymerization-dependent manner, and GTP-bound F-actin decorates with the myosin S1. Conversion of Phe(306) in the nucleotide binding site to the Tyr found in muscle actin raised the nucleotide discrimination ratio from the 1/9 of wild-type actin to 1/125. This result agrees with modeling that predicts that removal of the Tyr hydroxyl will create a space for the C2 amino group of the GTP guanine.
Authors:
Kuo-Kuang Wen; Xiaoyi Yao; Peter A Rubenstein
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.     Date:  2002-08-20
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Oct 
Date Detail:
Created Date:  2002-10-25     Completed Date:  2002-12-09     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  41101-9     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242, USA.
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MeSH Terms
Descriptor/Qualifier:
Actins / chemistry,  metabolism*
Adenosine Triphosphate / metabolism
Base Sequence
Cations, Divalent / metabolism
DNA Primers
Electrophoresis, Polyacrylamide Gel
Guanosine Triphosphate / metabolism*
Models, Molecular
Protein Binding
Saccharomyces cerevisiae / metabolism*
Grant Support
ID/Acronym/Agency:
AI 45728/AI/NIAID NIH HHS; GM 33689/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Actins; 0/Cations, Divalent; 0/DNA Primers; 56-65-5/Adenosine Triphosphate; 86-01-1/Guanosine Triphosphate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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