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

Mol Gen Genet. 1995 Feb 20;246(4):485-95. doi: 10.1007/BF00290452.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Cytoskeletal Proteins*
  • Cytoskeleton / metabolism*
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics*
  • Glycoside Hydrolases / metabolism
  • Molecular Sequence Data
  • Mutation
  • Nerve Tissue Proteins / chemistry
  • Phenotype
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid
  • beta-Fructofuranosidase


  • Actins
  • Cytoskeletal Proteins
  • Fungal Proteins
  • Nerve Tissue Proteins
  • RVS161 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • amphiphysin
  • Glycoside Hydrolases
  • beta-Fructofuranosidase