Analysis of a ptsH homologue from Streptomyces coelicolor A3(2) |
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Authors: | Michael J Butler Josef Deutscher Pieter W Postma T.J.Greer Wilson Anne Galinier Mervyn J Bibb |
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Affiliation: | Department of Genetics, John Innes Centre, Colney, Norwich NR4 7UH, UK;Laboratoire de Genetique des Microrganismes, INRA-CNRS ERS-567, F-78850 Thiverval-Grignon, France;EC Slater Institute, University of Amsterdam, Plantage Muidergracht 12, 1018 TV Amsterdam, The Netherlands;Department of Physiology, Carlsberg Laboratory, Copenhagen, Valby DK-2500, Denmark;Institut de Biologie et Chimie des Protéines, CNRS, 7 passage du Vercors, F-69367 Lyon Cedex 07, France |
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Abstract: | 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. |
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Keywords: | Carbon catabolite repression EI HPr HPr kinase PTS Streptomyces coelicolor A3(2) |
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