Isolation and characterization of Saccharomyces cerevisiae mutants resistant to aculeacin A.
AUTOR(ES)
Font de Mora, J
RESUMO
Aculeacin A is a lipopeptide that inhibits beta-glucan synthesis in yeasts. A number of Saccharomyces cerevisiae mutants resistant to this antibiotic were isolated, and four loci (ACR1, ACR2, ACR3, and ACR4) whose products are involved in the sensitivity to aculeacin A of yeast cells were defined. Mutants containing mutations in the four loci were also resistant to echinocandin B, another member of this lipopeptide family of antibiotics. In contrast, acr1, acr3, and acr4 mutants were resistant to papulacandin B (an antibiotic containing a disaccharide linked to two fatty acid chains that also inhibits beta-glucan synthesis), but acr2 mutants were susceptible to this antibiotic. This result defines common and specific steps in the entry and action of aculeacin A and papulacandin B. The analysis of double mutants revealed an epistatic effect of the acr2 mutation on the other three mutations. Cell walls of the four different mutants did not show significant alterations in composition with respect to the parental strain, and in vitro glucan synthase activity was also unaffected. However, cell surface hydrophobicity in three of the mutants was considerably decreased with respect to the parental strain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=245437Documentos Relacionados
- Isolation and characterization of Saccharomyces cerevisiae mutants resistant to Calcofluor white.
- Isolation and characterization of vanadate-resistant mutants of Saccharomyces cerevisiae.
- Isolation and characterization of aminopeptidase mutants of Saccharomyces cerevisiae.
- Isolation and characterization of Saccharomyces cerevisiae glycolytic pathway mutants.
- Isolation and Characterization of Mms-Sensitive Mutants of SACCHAROMYCES CEREVISIAE