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Table of Contents
Vol. 12, No. 1-2, 2007
Issue release date: December 2006
Section title: Paper
J Mol Microbiol Biotechnol 2007;12:67–74
(DOI:10.1159/000096461)

A New Piece of an Old Jigsaw: Glucose Kinase Is Activated Posttranslationally in a Glucose Transport-Dependent Manner in Streptomyces coelicolor A3(2)

van Wezel G.P.a · König M.b · Mahr K.b · Nothaft H.b, c · Thomae A.W.b, d · Bibb M.e · Titgemeyer F.b
aMicrobial Development, Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands; bDepartment of Mikrobiologie, Friedrich Alexander University Erlangen-Nürnberg, Erlangen, Germany; cInstitute for Biological Sciences National Research Council, Ottawa, Canada; dDepartment of Gene Vectors, GSF-National Research Center for Environment and Health, Munich, Germany; eDepartment of Molecular Microbiology, John Innes Centre, Norwich, UK

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Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: December 21, 2006
Issue release date: December 2006

Number of Print Pages: 8
Number of Figures: 5
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB

Abstract

Members of the soil-dwelling prokaryotic genus Streptomyces are indispensable for the recycling of complex polysaccharides, and produce a wide range of natural products. Nutrient limitation is likely to be a major signal for the onset of their development, resulting in spore formation by specialized aerial hyphae. Streptomycetes grow on numerous carbon sources, which they utilize in a preferential manner. The main signaling pathway underlying this phenomenon is carbon catabolite repression, which in streptomycetes is totally dependent on the glycolytic enzyme glucose kinase (Glk). How Glk exerts this fascinating dual role (metabolic and regulatory) is still largely a mystery. We show here that while Glk is made constitutively throughout the growth of Streptomyces coelicolor A3(2), its catalytic activity is modulated in a carbon source-dependent manner: while cultures growing exponentially on glucose exhibit high Glk activity, mannitol- grown cultures show negligible activity. Glk activity was directly proportional to the amount of two Glk isoforms observed by Western blot analysis. The activity profile of GlcP, the major glucose permease, correlated very well with that of Glk. Our data are consistent with a direct interaction between Glk and GlcP, suggesting that a Glk-GlcP permease complex is required for efficient glucose transport by metabolic trapping. This is supported by the strongly reduced accumulation of glucose in glucose kinase mutants. A model to explain our data is presented.

© 2007 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: December 21, 2006
Issue release date: December 2006

Number of Print Pages: 8
Number of Figures: 5
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB


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Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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