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Originally published In Press as doi:10.1074/jbc.M108303200 on February 11, 2002

J. Biol. Chem., Vol. 277, Issue 17, 14986-14995, April 26, 2002
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A Nucleotide Switch in the Escherichia coli DnaA Protein Initiates Chromosomal Replication
EVIDENCE FROM A MUTANT DnaA PROTEIN DEFECTIVE IN REGULATORY ATP HYDROLYSIS IN VITRO AND IN VIVO*

Satoshi NishidaDagger §, Kazuyuki FujimitsuDagger , Kazuhisa Sekimizu, Tadahiro Ohmura||, Tadashi Ueda||, and Tsutomu KatayamaDagger **

From the Dagger  Department of Molecular Microbiology and the || Department of Immunology, Kyushu University Graduate School of Pharmaceutical Sciences, Higashi-ku, Fukuoka 812-8582, Japan and the  Department of Developmental Biochemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

The ATP-bound DnaA protein opens duplex DNA at the Escherichia coli origin of replication, leading to a series of initiation reactions in vitro. When loaded on DNA, the DNA polymerase III sliding clamp stimulates hydrolysis of DnaA-bound ATP in the presence of the IdaB/Hda protein, thereby yielding ADP-DnaA, which is inactive for initiation in vitro. This negative feedback regulation of DnaA activity is proposed to play a crucial role in the replication cycle. We here report that the mutant protein DnaA R334A is inert to hydrolysis of bound ATP, although its affinities for ATP and ADP remain unaffected. The ATP-bound DnaA R334A protein, but not the ADP form, initiates minichromosomal replication in vitro at a level similar to that seen for wild-type DnaA. When expressed at moderate levels in vivo, DnaA R334A is predominantly in the ATP-bound form, unlike the wild-type and DnaA E204Q proteins, which in vitro hydrolyze ATP in a sliding clamp- and IdaB/Hda-dependent manner. Furthermore, DnaA R334A, but not the wild-type or the DnaA E204Q proteins, promotes overinitiation of chromosomal replication. These in vivo data support a crucial role for bound nucleotides in regulating the activity of DnaA during replication. Based on a homology modeling analysis, we suggest that the Arg-334 residue closely interacts with bound nucleotides.

* This work was supported in part by research grants from the Japan Society for the Promotion of Science and the Ministry of Education, Culture, Sports, Technology and Science of Japan.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.

§ Present address: Dept. of Infectious Diseases Research, National Children's Medical Research Center, Setagaya-ku, Tokyo 154-8509, Japan.

** To whom correspondence should be addressed: Dept. of Molecular Microbiology, Kyushu University Graduate School of Pharmaceutical Sciences, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. Tel.: 81-92-642-6644; Fax: 81-92-642-6646; E-mail: katayama@phar.kyushu- u.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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