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PMID: 8334302 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Unexpected combinations of null mutations in genes encoding the actin cytoskeleton are lethal in yeast.

Molecular biology of the cell ·Vol. 4 ·No. 5 ·1993-05-00 ·Pages 459-68

Adams AE, Cooper JA, Drubin DG

Abstract

To understand the role of the actin cytoskeleton in cell physiology, and how actin-binding proteins regulate the actin cytoskeleton in vivo, we and others previously identified actin-binding proteins in Saccharomyces cerevisiae and studied the effect of null mutations in the genes for these proteins. A null mutation of the actin gene (ACT1) is lethal, but null mutations in the tropomyosin (TPM1), fimbrin (SAC6), Abp1p (ABP1), and capping protein (CAP1 and CAP2) genes have relatively mild or no effects. We have now constructed double and triple mutants lacking 2 or 3 of these actin-binding proteins, and studied the effect of the combined mutations on cell growth, morphology, and organization of the actin cytoskeleton. Double mutants lacking fimbrin and either Abp1p or capping protein show negative synthetic effects on growth, in the most extreme case resulting in lethality. All other combinations of double mutations and the triple mutant lacking tropomyosin, Abp1p, and capping protein, are viable and their phenotypes are similar to or only slightly more severe than those of the single mutants. Therefore, the synthetic phenotypes are highly specific. We confirmed this specificity by overexpression of capping protein and Abp1p in strains lacking fimbrin. Thus, while overexpression of these proteins has deleterious effects on actin organization in wild-type strains, no synthetic phenotype was observed in the absence of fimbrin. We draw two important conclusions from these results. First, since mutations in pairs of actin-binding protein genes cause inviability, the actin cytoskeleton of yeast does not contain a high degree of redundancy. Second, the lack of structural and functional homology among these genetically redundant proteins (fimbrin and capping protein or Abp1p) indicates that they regulate the actin cytoskeleton by different mechanisms. Determination of the molecular basis for this surprising conclusion will provide unique insights into the essential mechanisms that regulate the actin cytoskeleton.

Related Genes
MeSH Terms
Actin Depolymerizing Factors Actins/metabolism Cytoskeleton/chemistry,ultrastructure Destrin Genes, Fungal Genes, Lethal Membrane Glycoproteins/genetics Microfilament Proteins/genetics Microscopy, Fluorescence Mutation Phenotype Saccharomyces cerevisiae/genetics,growth & development,ultrastructure Suppression, Genetic
Chemicals
Actin Depolymerizing Factors Actins Destrin Membrane Glycoproteins Microfilament Proteins plastin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Adams A E
Department of Molecular and Cellular Biology, Life Sciences South, University of Arizona, Tuscon 85721.
Cooper J A
Drubin D G
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
1993-05-00
Pages
459-68
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC300950
Subset
IM
Grants
NIGMS NIH HHS · GM38542 · United States
NIGMS NIH HHS · GM42759 · United States
NIGMS NIH HHS · GM45288 · United States
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