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Papers In Press, published online ahead of print February 11, 2002
Department of Molecular Microbiology, Kyushu University, Fukuoka 812-8582
Corresponding Author: katayama{at}phar.kyushu-u.ac.jp
The ATP-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 with the 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 by the DnaA E204Q proteins, promotes overinitiation of chromosomal replication. This in vivo data supports a crucial role for bound nucleotides in regulating the activity of DnaA during replication. Based on a homology modeling analysis, we suggest that the R334 residue closely interacts with bound nucleotides.
J. Biol. Chem, 10.1074/jbc.M108303200
Submitted on August 28, 2001
Revised on December 19, 2001
Accepted on February 10, 2002
A nucleotide switch in the E. coli DnaA protein initiates chromosomal replication: Evidence from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo
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