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J Biol Chem, Vol. 275, Issue 3, 1773-1780, January 21, 2000
From the Carbon catabolite repression allows bacteria to
rapidly alter the expression of catabolic genes in response to the
availability of metabolizable carbon sources. In Bacillus
subtilis, this phenomenon is controlled by the HPr kinase (HprK)
that catalyzes ATP-dependent phosphorylation of either HPr
(histidine containing protein) or Crh (catabolite repression HPr) on
residue Ser-46. We report here that B. subtilis HprK forms
homo-oligomers constituted most likely of eight subunits. Related to
this complex structure, the enzyme displays strong positive
cooperativity for the binding of its allosteric activator, fructose
1,6-bisphosphate, as evidenced by either kinetics of its
phosphorylation activity or the intrinsic fluorescence properties of
its unique tryptophan residue, Trp-235. It is further shown that
activation of HPr phosphorylation by fructose 1,6-bisphosphate
essentially occurs at low ATP and enzyme concentrations. A positive
cooperativity was also detected for the binding of natural nucleotides
or their 2'(3')-N-methylanthraniloyl derivatives, in either
phosphorylation or fluorescence experiments. Most interestingly,
quenching of the HprK tryptophan fluorescence by using either iodide or
acrylamide revealed a heterogeneity of tryptophan residues within the
population of oligomers, suggesting that the enzyme exists in two
different conformations. This result suggests a concerted-symmetry
model for the catalytic mechanism of positive cooperativity displayed
by HprK.
The HPr Kinase from Bacillus subtilis Is a
Homo-oligomeric Enzyme Which Exhibits Strong Positive Cooperativity for
Nucleotide and Fructose 1,6-Bisphosphate Binding*
,,,
Institut de Biologie et Chimie des
Protéines, UPR 412 CNRS, 69367 Lyon Cedex 07, France, the
§ Laboratoire d'Enzymologie et de Biochimie Structurales,
UPR 9063 CNRS, bât. 34, 91198 Gif-sur-Yvette, France, and the
¶ Laboratoire de Génétique des Microorganismes, INRA
and CNRS ERS-567, 78850 Thiverval-Grignon, France
*
This work was supported by the CNRS, the Université de
Lyon, and the Université d'Orsay.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Institut de
Biologie et Chimie des Protéines, UPR 412 CNRS, 7 Passage du
Vercors, F-69367 Lyon Cedex 07, France. E-mail: a.galinier@ibcp.fr;
Tel.: 33-472722679; Fax: 33-472722601.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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