Stable nucleotide binding to DnaA requires a specific glutamic acid residue within the AAA+ box II motif

Journal of Structural Biology
Shogo OzakiTsutomu Katayama

Abstract

In complex with ATP, but not ADP, DnaA protein multimers unwind a specific region of duplex DNA within the chromosomal replication origin, oriC, triggering a series of reactions that result in initiation of DNA replication. Following replication initiation, ATP hydrolysis, which is coupled to DNA replication, results in the generation of initiation-incompetent ADP-DnaA. Suppression of overinitiation of replication requires that ADP-DnaA complexes be stably maintained until the next round of replication. Thus, the functional and structural requirements that ensure stable nucleotide binding to DnaA are crucial for proper regulation of replication. Here, we demonstrate that Glu143 of DnaA, located within the AAA+ box II N-linker motif, is a key residue involved in stable nucleotide binding. A Glu143 substitution variant of DnaA (DnaA E143A) bound to ADP on ice with an affinity similar to wild-type DnaA, but the resultant ADP-DnaA E143A complex was more labile at 37 °C than wild-type ADP-DnaA complexes. Consistent with this, conversion of ADP-DnaA E143A to ATP-DnaA E143A was stimulated at 37°C in the presence of ATP, which also stimulated replication of a minichromosome in an in vitro reconstitution reaction. Expression of DnaA E14...Continue Reading

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Citations

Aug 27, 2016·Frontiers in Molecular Biosciences·Katarzyna E WegrzynIgor Konieczny
Jan 10, 2018·Frontiers in Microbiology·Tsutomu KatayamaHironori Kawakami
May 18, 2013·Environmental Microbiology·Masayuki Su'etsuguTsutomu Katayama

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