Note. The novel nucleotide sequence data published here have been deposited with the EMBL sequence data bank and are available under the accession number X75485. The novel amino acid sequence data have also been deposited with the Swiss-Prot sequence data bank.
PPQ, a novel protein phosphatase containing a Ser+Asn-rich amino-terminal domain, is involved in the regulation of protein synthesis
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 218, Issue 2, pages 689–699, December 1993
How to Cite
CHEN, M. X., CHEN, Y. H. and COHEN, P. T. W. (1993), PPQ, a novel protein phosphatase containing a Ser+Asn-rich amino-terminal domain, is involved in the regulation of protein synthesis. European Journal of Biochemistry, 218: 689–699. doi: 10.1111/j.1432-1033.1993.tb18423.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received August 25, 1993) – EJB 93 1288/6
The sequence of a Saccharomyces cerevisiae cDNA encoding a novel 61-kDa protein serine/threonine phosphatase, termed PPQ1, is presented. The protein consists of two distinct domains: the carboxy-terminal phosphatase domain is approximately 60% identical to either PP1 or the carboxy-terminal domains of PPZ1 and PPZ2, while the amino-terminal region is rich in serine and asparagine. Deletion of the gene encoding PPQ1 reduces cell growth on several carbon sources, and lowers cell density in the stationary phase. Cells in which PPQ1 gene has been deleted show altered morphology from wild-type cells in the stationary phase in the absence of an essential amino acid and a reduced rate of protein synthesis in the exponential phase. They are hypersensitive to the protein synthesis inhibitors, cycloheximide and G418, implicating PPQ1 in the regulation of translation.