Open AccessAnalysis of a ptsH homologue from Streptomyces coelicolor A3(2)
Author(s) -
Butler Michael J,
Deutscher Josef,
Postma Pieter W,
Wilson T.J.Greer,
Galinier Anne,
Bibb Mervyn J
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13744.x
Subject(s) - streptomyces coelicolor , catabolite repression , bacillus subtilis , galactokinase , biology , biochemistry , streptomyces , escherichia coli , streptomycetaceae , pep group translocation , microbiology and biotechnology , gene , actinomycetales , genetics , bacteria , mutant
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.