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Transcription Regulators Potentially Controlled by HPr Kinase/Phosphorylase in Gram-Negative Bacteria

Boël G.a · Mijakovic I.a · Mazé A.a · Poncet S.a · Taha M.-K.b · Larribe M.b · Darbon E.a · Khemiri A.a · Galinier A.c · Deutscher J.a

Author affiliations

aMicrobiologie et Génétique Moléculaire, CNRS UMR2585, Thiverval-Grignon, bUnité des Neisseria, Institut Pasteur, Paris, et cLaboratoire de Chimie Bactérienne, Institut de Biologie Structurale et Microbiologie, CNRS UPR9043, Marseille, France

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J Mol Microbiol Biotechnol 2003;5:206–215

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Article / Publication Details

First-Page Preview
Abstract of Minireview

Published online: July 16, 2003
Issue release date: July 2003

Number of Print Pages: 10
Number of Figures: 4
Number of Tables: 1

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

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

Abstract

Phosphorylation and dephosphorylation at Ser-46 in HPr, a phosphocarrier protein of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) is controlled by the bifunctional HPr kinase/phosphorylase (HprK/P). In Gram-positive bacteria, P-Ser-HPr controls (1) sugar uptake via the PTS; (2) catabolite control protein A (CcpA)-mediated carbon catabolite repression, and (3) inducer exclusion. Genome sequencing revealed that HprK/P is absent from Gram-negative enteric bacteria, but present in many other proteobacteria. These organisms also possess (1) HPr, the substrate for HprK/P; (2) enzyme I, which phosphorylates HPr at His-15, and (3) one or several enzymes IIA, which receive the phosphoryl group from P∼His-HPr. The genes encoding the PTS proteins are often organized in an operon with hprK. However, most of these organisms miss CcpA and a functional PTS, as enzymes IIB and membrane-integrated enzymes IIC seem to be absent. HprK/P and the rudimentary PTS phosphorylation cascade in Gram-negative bacteria must therefore carry out functions different from those in Gram-positive organisms. The gene organization in many HprK/P-containing Gram-negative bacteria as well as some preliminary experiments suggest that HprK/P might control transcription regulators implicated in cell adhesion and virulence. In α-proteobacteria, hprK is located downstream of genes encoding a two-component system of the EnvZ/OmpR family. In several other proteobacteria, hprK is organized in an operon together with genes from the rpoN region of Escherichia coli (rpoN encodes a σ54). We propose that HprK/P might control the phosphorylation state of HPr and EIIAs, which in turn could control the transcription regulators.

© 2003 S. Karger AG, Basel


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Article / Publication Details

First-Page Preview
Abstract of Minireview

Published online: July 16, 2003
Issue release date: July 2003

Number of Print Pages: 10
Number of Figures: 4
Number of Tables: 1

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

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


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