Regulation of yeast actin behavior by interaction of charged residues across the interdomain cleft

Xiaoyi Yao; Vinh Nguyen; Willy Wriggers; Peter A Rubenstein

doi:10.1074/jbc.M201685200

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Regulation of yeast actin behavior by interaction of charged residues across the interdomain cleft

Journal article

Open access

Peer reviewed

Regulation of yeast actin behavior by interaction of charged residues across the interdomain cleft

Xiaoyi Yao, Vinh Nguyen, Willy Wriggers and Peter A Rubenstein

The Journal of biological chemistry, Vol.277(25), pp.22875-22882

06/21/2002

DOI: 10.1074/jbc.M201685200

PMID: 11940592

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Abstract

His(73) participates in the regulation of the nucleotide binding cleft conformation in yeast actin. Earlier molecular dynamics studies suggested that Asp(184) interacts with His(73) thereby stabilizing a "closed-cleft" G-actin. However, beta-actin in the open-cleft state shows a closer interaction of His(73) with Asp(179) than with Asp(184). We have thus assessed the relative importance of Asp(184) and Asp(179) on yeast actin stability and function. Neutral substitutions at 184 or 179 alone had little adverse effect on the monomer and polymerization behavior of actin. Arg or His at 184 in H73E actin partially rescued the monomeric properties of H73E actin, as demonstrated by near-normal thermostability and wild-type (WT)-like protease digestion patterns. ATP exchange was still considerably faster than with WT-actin although slower than that of H73E alone. However, polymerization of H73E/D184R and H73E/D184H is worse than with H73E alone. Conversely, D179R rescued all monomeric properties of H73E to near WT values and largely restored polymerization rate and filament thermostability. These results and new simulations of G-actin in the "open" state underscore the importance of the His(73)-Asp(179) interaction and suggest that the open and not the closed state of yeast actin may be favored in the absence of the methyl group of His(73).

Protein Structure, Tertiary

Temperature

Mutagenesis, Site-Directed

Actins - metabolism

Models, Molecular

Dose-Response Relationship, Drug

Time Factors

Adenosine Triphosphate - metabolism

Methylhistidines - chemistry

Protein Binding

Aspartic Acid - metabolism

Protein Conformation

Aspartic Acid - chemistry

Mutation

Histidine - chemistry

Fungal Proteins - metabolism

Details

Title: Subtitle: Regulation of yeast actin behavior by interaction of charged residues across the interdomain cleft
Creators: Xiaoyi Yao - Department of Biochemistry, University of Iowa College of Medicine, Iowa City, Iowa 52242, USA
Vinh Nguyen
Willy Wriggers
Peter A Rubenstein
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.277(25), pp.22875-22882
DOI: 10.1074/jbc.M201685200
PMID: 11940592
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: GM33689 / NIGMS NIH HHS P41RR12255 / NCRR NIH HHS
Language: English
Date published: 06/21/2002
Academic Unit: Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9984025278702771

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