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J Biol Chem, Vol. 274, Issue 52, 37443-37449, December 24, 1999

His73, Often Methylated, Is an Important Structural Determinant for Actin
A MUTAGENIC ANALYSIS OF HIS73 OF YEAST ACTIN*

Xiaoyi Yao, Stephanie Grade, Willy WriggersDagger §, and Peter A. Rubenstein

From the Department of Biochemistry, University of Iowa College of Medicine, Iowa City, Iowa 52242 and the Dagger  Department of Chemistry and Biochemistry, University of California, San Diego, California 92093

His73, has been proposed to regulate the release of Pi from the interior of actin following polymerization-dependent hydrolysis of bound ATP. Although it is a 3-methylhistidine in the vast majority of actins, His73 is unmethylated in S. cerevisiae actin. We mutated His73 in yeast actin to Arg, Lys, Ala, Gln, and Glu and detected no altered phenotypes associated with the mutations in vivo. However, they significantly affect actin function in vitro. Substitution of the more basic residues resulted in enhanced thermal stability, decreased rate of nucleotide exchange, and decreased susceptibility to controlled proteolysis relative to wild-type actin. The opposite effects are observed with the neutral and anionic substitutions. All mutations reduced the rate of polymerization. Molecular dynamics simulations predict a new conformation for the His73 imidazole in the absence of a methyl group. It also predicts that Arg73 tightens and stabilizes the actin and that Glu73 causes a rearrangement of the bottom of actin's interdomain cleft leading possibly to our observed destabilization of actin. Considering the exterior location of His73, this work indicates a surprisingly important role for the residue as a major structural determinant of actin and provides a clue to the impact caused by methylation of His73.

* This work was supported in part by National Institutes of Health Grant GM33689 (to P. A. R.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported in part by National Institute of Health grants to Ronald A. Milligan (Scripps Research Institute) and J. Andrew McCammon, (University of California, San Diego) and by the La Jolla Interfaces in Science Interdisciplinary Training Program/Burroughs Wellcome.

To whom correspondence should be addressed: Dept. of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242. Tel.: 319-335-7911; Fax: 319-335-9570.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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