JBC GenomeOne product landing page

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/17/14986    most recent
M108303200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nishida, S.
Right arrow Articles by Katayama, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nishida, S.
Right arrow Articles by Katayama, T.

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.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
S. Ozaki, H. Kawakami, K. Nakamura, N. Fujikawa, W. Kagawa, S.-Y. Park, S. Yokoyama, H. Kurumizaka, and T. Katayama
A Common Mechanism for the ATP-DnaA-dependent Formation of Open Complexes at the Replication Origin
J. Biol. Chem., March 28, 2008; 283(13): 8351 - 8362.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Siddiqui and B. Stillman
ATP-dependent Assembly of the Human Origin Recognition Complex
J. Biol. Chem., November 2, 2007; 282(44): 32370 - 32383.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
K. Keyamura, N. Fujikawa, T. Ishida, S. Ozaki, M. Su'etsugu, K. Fujimitsu, W. Kagawa, S. Yokoyama, H. Kurumizaka, and T. Katayama
The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes
Genes & Dev., August 15, 2007; 21(16): 2083 - 2099.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Abe, T. Jo, Y. Matsuda, C. Matsunaga, T. Katayama, and T. Ueda
Structure and Function of DnaA N-terminal Domains: SPECIFIC SITES AND MECHANISMS IN INTER-DnaA INTERACTION AND IN DnaB HELICASE LOADING ON oriC
J. Biol. Chem., June 15, 2007; 282(24): 17816 - 17827.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
L. Riber, J. A. Olsson, R. B. Jensen, O. Skovgaard, S. Dasgupta, M. G. Marinus, and A. Lobner-Olesen
Hda-mediated inactivation of the DnaA protein and dnaA gene autoregulation act in concert to ensure homeostatic maintenance of the Escherichia coli chromosome
Genes & Dev., August 1, 2006; 20(15): 2121 - 2134.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
S. Ozaki, K. Fujimitsu, H. Kurumizaka, and T. Katayama
The DnaA homolog of the hyperthermophilic eubacterium Thermotoga maritima forms an open complex with a minimal 149-bp origin region in an ATP-dependent manner
Genes Cells, April 1, 2006; 11(4): 425 - 438.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M.-F.ço. Noirot-Gros, M. Velten, M. Yoshimura, S. McGovern, T. Morimoto, S. D. Ehrlich, N. Ogasawara, P. Polard, and P. Noirot
Functional dissection of YabA, a negative regulator of DNA replication initiation in Bacillus subtilis
PNAS, February 14, 2006; 103(7): 2368 - 2373.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. I. Goranov, L. Katz, A. M. Breier, C. B. Burge, and A. D. Grossman
A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA
PNAS, September 6, 2005; 102(36): 12932 - 12937.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Kawakami, K. Keyamura, and T. Katayama
Formation of an ATP-DnaA-specific Initiation Complex Requires DnaA Arginine 285, a Conserved Motif in the AAA+ Protein Family
J. Biol. Chem., July 22, 2005; 280(29): 27420 - 27430.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
O. Skovgaard and A. Lobner-Olesen
Reduced initiation frequency from oriC restores viability of a temperature-sensitive Escherichia coli replisome mutant
Microbiology, March 1, 2005; 151(3): 963 - 973.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Su'etsugu, T.-r. Shimuta, T. Ishida, H. Kawakami, and T. Katayama
Protein Associations in DnaA-ATP Hydrolysis Mediated by the Hda-Replicase Clamp Complex
J. Biol. Chem., February 25, 2005; 280(8): 6528 - 6536.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
T.-r. Shimuta, K. Nakano, Y. Yamaguchi, S. Ozaki, K. Fujimitsu, C. Matsunaga, K. Noguchi, A. Emoto, and T. Katayama
Novel heat shock protein HspQ stimulates the degradation of mutant DnaA protein in Escherichia coli
Genes Cells, December 1, 2004; 9(12): 1151 - 1166.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Ishida, N. Akimitsu, T. Kashioka, M. Hatano, T. Kubota, Y. Ogata, K. Sekimizu, and T. Katayama
DiaA, a Novel DnaA-binding Protein, Ensures the Timely Initiation of Escherichia coli Chromosome Replication
J. Biol. Chem., October 29, 2004; 279(44): 45546 - 45555.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
M. Kurz, B. Dalrymple, G. Wijffels, and K. Kongsuwan
Interaction of the Sliding Clamp {beta}-Subunit and Hda, a DnaA-Related Protein
J. Bacteriol., June 1, 2004; 186(11): 3508 - 3515.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
M. Su'etsugu, M. Takata, T. Kubota, Y. Matsuda, and T. Katayama
Molecular mechanism of DNA replication-coupled inactivation of the initiator protein in Escherichia coli: interaction of DnaA with the sliding clamp-loaded DNA and the sliding clamp-Hda complex
Genes Cells, June 1, 2004; 9(6): 509 - 522.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
Y. Oku, K. Kurokawa, N. Ichihashi, and K. Sekimizu
Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol
Microbiology, January 1, 2004; 150(1): 45 - 51.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
R. Kruger and M. Filutowicz
{pi} Protein- and ATP-dependent transitions from 'closed' to 'open' complexes at the {gamma} ori of plasmid R6K
Nucleic Acids Res., October 15, 2003; 31(20): 5993 - 6003.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
A. Blinkova, M. J. Hermandson, and J. R. Walker
Suppression of Temperature-Sensitive Chromosome Replication of an Escherichia coli dnaX(Ts) Mutant by Reduction of Initiation Efficiency
J. Bacteriol., June 15, 2003; 185(12): 3583 - 3595.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.