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J Biol Chem, Vol. 274, Issue 50, 35873-35880, December 10, 1999
From the Department of Biochemistry, University of Iowa College of
Medicine, Iowa City, Iowa 52242-1104
A mutant yeast actin (GG) has decreased
hydrophobicity in a subdomain 3/4 hydrophobic plug believed to be
involved in a hydrophobic cross-strand "plug-pocket" interaction
necessary for actin filament stability. This actin will not polymerize
in vitro but is compatible with cell viability. We have
assessed the ability of Sac6p, the yeast homologue of the actin
filament stabilizing and bundling protein fimbrin, to restore
polymerization in vitro and to facilitate GG-actin function
in vivo. Sac6p rescues GG-actin polymerization at 25 °C
but not at 4 °C. The actin polymerizes into bundles at room
temperature with a fimbrin:actin molar ratio of 1:4. At this ratio,
every actin monomer contacts a Sac6p actin binding domain. Following
cold-induced depolymerization, actin/Sac6p mixtures repolymerize
beginning at 15 °C instead of the 25 °C required for de
novo assembly, because of the presence of residual actin-Sac6p nuclei. Generation of haploid 
sac6/GG-actin cells from either diploid or haploid cells was unsuccessful. The facile isolation of
cells with either mutation alone indicates a synthetic lethal relationship between this actin allele and the SAC6 gene.
Sac6p may allow GG-actin function in vivo by stabilizing
the actin in bundles thereby helping maintain sufficient levels of an
otherwise destabilized actin monomer within the cell.
To whom correspondence should be addressed. Tel.: 319-335-7911;
Fax: 319-335-9570; E-mail: peter-rubenstein@uiowa.edu.
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