期刊
JOURNAL OF BACTERIOLOGY
卷 182, 期 19, 页码 5634-5638出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.182.19.5634-5638.2000
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We cloned the yloO gene and purified a sis-tagged form of its product, the putative protein phosphatase YloO, which we nom designate PrpC. This closely resembles the human protein phosphatase PP2C, a member of the PPM family, in sequence and predicted secondary structure, PrpC has phosphatase activity in vitro against a synthetic substrate, p-nitrophenol phosphate, and endogenous Bacillus subtilis proteins. The prkC and prpC genes are adjacent on the chromosome, and the phosphorylated form of PrkC is a substrate for PrpC, These findings suggest that PrkC and PrpC may function as a couple in vivo.
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