Ogawa N, Tzeng C M, Fraley C D, Kornberg A
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA.
J Bacteriol. 2000 Dec;182(23):6687-93. doi: 10.1128/JB.182.23.6687-6693.2000.
Vibrio cholerae O1, biotype El Tor, accumulates inorganic polyphosphate (poly P) principally as large clusters of granules. Poly P kinase (PPK), the enzyme that synthesizes poly P from ATP, is encoded by the ppk gene, which has been cloned from V. cholerae, overexpressed, and knocked out by insertion-deletion mutagenesis. The predicted amino acid sequence of PPK is 701 residues (81.6 kDa), with 64% identity to that of Escherichia coli, which it resembles biochemically. As in E. coli, ppk is part of an operon with ppx, the gene that encodes exopolyphosphatase (PPX). However, unlike in E. coli, PPX activity was not detected in cell extracts of wild-type V. cholerae. The ppk null mutant of V. cholerae has diminished adaptation to high concentrations of calcium in the medium as well as motility and abiotic surface attachment.
霍乱弧菌O1型,埃尔托生物型,主要以大颗粒簇的形式积累无机多聚磷酸盐(多聚P)。多聚P激酶(PPK)是一种由ATP合成多聚P的酶,由ppk基因编码,该基因已从霍乱弧菌中克隆、过表达,并通过插入缺失诱变被敲除。PPK的预测氨基酸序列为701个残基(81.6 kDa),与大肠杆菌的序列有64%的同源性,在生化性质上与之相似。与大肠杆菌一样,ppk是一个操纵子的一部分,该操纵子包含ppx,即编码外多聚磷酸酶(PPX)的基因。然而,与大肠杆菌不同的是,在野生型霍乱弧菌的细胞提取物中未检测到PPX活性。霍乱弧菌的ppk基因缺失突变体对培养基中高浓度钙的适应性、运动性和非生物表面附着能力均有所下降。