Mx. Chen et al., PPQ, A NOVEL PROTEIN PHOSPHATASE CONTAINING A SER PLUS ASN-RICH AMINO-TERMINAL DOMAIN, IS INVOLVED IN THE REGULATION OF PROTEIN-SYNTHESIS, European journal of biochemistry, 218(2), 1993, pp. 689-699
The sequence of a Saccharomyces cerevisiae cDNA encoding a novel 61-kD
a protein serine/threonine phosphatase, termed PPQ1, is presented. The
protein consists of two distinct domains: the carboxy-terminal phosph
atase domain is approximately 60% identical to either PP1 or the carbo
xy-terminal domains of PPZ1 and PPZ2, while the amino-terminal region
is rich in serine and asparagine. Deletion of the gene encoding PPQ1 r
educes cell growth on several carbon sources, and lowers cell density
in the stationary phase. Cells in which PPQ1 gene has been deleted sho
w altered morphology from wild-type cells in the stationary phase in t
he absence of an essential amino acid and a reduced rate of protein sy
nthesis in the exponential phase. They are hypersensitive to the prote
in synthesis inhibitors, cycloheximide and G418, implicating PPQ1 in t
he regulation of translation.