SACCHAROMYCES-CEREVISIAE PROTEIN INVOLVED IN PLASMID MAINTENANCE IS NECESSARY FOR MATING OF MAT-ALPHA CELLS
SACCHAROMYCES-CEREVISIAE PROTEIN INVOLVED IN PLASMID MAINTENANCE IS NECESSARY FOR MATING OF MAT-ALPHA CELLS
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DOI:
10.1016/0022-2836(88)90358-0
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发表时间:
1988-12-05
影响因子:
5.6
通讯作者:
TYE, BK
中科院分区:
文献类型:
--
作者:
PASSMORE, S;MAINE, GT;TYE, BK
We previously reported the isolation of yeast mutants that seem to affect the function of certain autonomously replicating sequences (ARSs). These mutants are known asmcmfor their defect in the maintenance of minichromosomes. We have now characterized in more detail oneARS-specific mutation,mcm1-1. This Mcm1 mutant has a second phenotype;MATαmcm1-1 strains are sterile.MCM1 is non-allelic to other known α-specific sterile mutations and, unlike most genes required for mating, it is essential for growth. The α-specific sterile phenotype of themcm1-1 mutant is manifested by its failure to produce a normal amount of the mating pheromone, α-factor. In addition, transcripts of theMFα1 andSTE3 genes, which encode the α-factor precursor and thea-factor receptor, respectively, are greatly reduced in this mutant. These and other properties of themcm1-1 mutant suggest that theMCM1 protein may act as a transcriptional activator of α-specific genes.We have cloned, mapped and sequenced the wild-type and mutant alleles ofMCM1, which is located on the right arm of chromosome XIII nearLYS7. TheMCM1 gene product is a protein of 286 amino acid residues and contains an unusual region in which 19 out of 20 residues are either aspartic or glutamic acid, followed by a series of glutamine tracts.MCM1 has striking homology toARG80, a regulatory gene of the arginine metabolic pathway located about 700 base-pairs upstream fromMCM1. A substitution of leucine for proline at amino acid position 97, immediately preceding the polyanionic region, was shown to be responsible for both the α-specific sterile and minichromosome-maintenance defective phenotypes of themcm1-1 mutant.