Analysis of a ptsH homologue from Streptomyces coelicolor A3(2)

被引:21
作者
Butler, MJ
Deutscher, J
Postma, PW
Wilson, TJG
Galinier, A
Bibb, MJ [1 ]
机构
[1] John Innes Ctr Plant Sci Res, Dept Genet, Norwich NR4 7UH, Norfolk, England
[2] INRA, Lab Genet Microorganismes, CNRS, F-78850 Thiverval Grignon, France
[3] Univ Amsterdam, EC Slater Inst Biochem Res, NL-1018 TV Amsterdam, Netherlands
[4] Carlsberg Lab, Dept Physiol, DK-2500 Copenhagen, Denmark
[5] CNRS, Inst biol & Chim Prot, F-69367 Lyon 07, France
基金
英国生物技术与生命科学研究理事会;
关键词
carbon catabolite repression; EI; HPr; HPr kinase; PTS; Streptomyces coelicolor A3(2);
D O I
10.1016/S0378-1097(99)00328-6
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A ptsH homologue of Streptomyces coelicolor A3(2) was identified in the emerging genome sequence, cloned in Escherichia coli and the S. coelicolor HPr over-produced and purified. The protein was phosphorylated in vitro in a phosphoenolpyruvate (PEP)-dependent manner by purified enzyme I (EI) from Bacillus subtilis, and much less efficiently in an ATP-dependent manner by purified HPr kinase, also from B. subtilis. There was no indication of ATP-dependent phosphorylation of the purified protein by cell extracts of either S. coelicolor or Streptomyces lividans. Deletion of the ptsH homologue from the S. coelicolor and S. lividans chromosomes had no effect on growth when fructose was supplied as sole carbon source, and in S. coelicolor it had no effect on glucose repression of agarase and galactokinase synthesis, suggesting that the HPr encoded by this gene does not play an essential role in fructose transport nor a general role in carbon catabolite repression. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:279 / 288
页数:10
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