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PMID: 7891662 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin.

Molecular & general genetics : MGG ·Vol. 246 ·No. 4 ·1995-02-20 ·Pages 485-95

Sivadon P, Bauer F, Aigle M, Crouzet M

Abstract

The actin cytoskeleton cells is altered in rvs161 mutant yeast, with the defect becoming more pronounced under unfavorable growth conditions, as described for the rvs167 mutant. The cytoskeletal alteration has no apparent effect on invertase secretion and polarized growth. Mutations in RVS161, just as in RVS167, lead to a random budding pattern in a/alpha diploid cells. This behavior is not observed in a/a diploid cells homozygous for the rvs161-1 or rvs167-1 mutations. In addition, sequence comparisons revealed that amphiphysin, a protein first found in synaptic vesicles of chicken and shown to be the autoantigen of Stiff Man syndrome, presents similarity with both Rvs proteins. Furthermore, limited similarities with myosin heavy chain and tropomyosin alpha chain from higher eukaryotic cells allow for the definition of a possible consensus sequence. The finding of related sequences suggests the existence of a function for these proteins that is conserved among eukaryotic organisms.

Related Genes
BUD3 BUD4
MeSH Terms
Actins/metabolism Amino Acid Sequence Cytoskeletal Proteins Cytoskeleton/metabolism Fungal Proteins/chemistry,genetics Glycoside Hydrolases/metabolism Molecular Sequence Data Mutation Nerve Tissue Proteins/chemistry Phenotype Saccharomyces cerevisiae/genetics,growth & development,metabolism Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid beta-Fructofuranosidase
Chemicals
Actins Cytoskeletal Proteins Fungal Proteins Nerve Tissue Proteins RVS161 protein, S cerevisiae Saccharomyces cerevisiae Proteins amphiphysin Glycoside Hydrolases beta-Fructofuranosidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sivadon P
Laboratoire de Génétique, CNRS UPR 9026, Université de Bordeaux II, Talence, France.
Bauer F
Aigle M
Crouzet M
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Article Info
Journal
Molecular & general genetics : MGG
Abbr.
Mol Gen Genet
ISSN
0026-8925
DOI
10.1007/BF00290452
Published
1995-02-20
Pages
485-95
Language
English
Region
Germany
NLM ID
0125036
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00290452
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