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YabA and DnaD inhibit helix assembly of the DNA replication initiation protein DnaA
Author(s) -
Scholefield Graham,
Murray Heath
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12353
Subject(s) - dnaa , biology , bacillus subtilis , dna replication , dna , dna binding protein , microbiology and biotechnology , seqa protein domain , origin of replication , origin recognition complex , biochemistry , genetics , bacteria , eukaryotic dna replication , transcription factor , gene
Summary Control of DNA replication initiation is essential for cell growth. A unifying characteristic of DNA replication initiator proteins is their distinctive AAA + nucleotide‐binding domains. The bacterial initiator DnaA assembles into a right‐handed helical oligomer built upon interactions between neighbouring AAA + domains to form an active initiation complex. Recently we developed a unique cross‐linking assay that specifically detects ATP ‐dependent DnaA helix assembly. Here we have utilized this assay to show that two DnaA regulatory proteins in B acillus subtilis , YabA and DnaD , inhibit DnaA helix formation. These results, in combination with our previous finding that the regulatory factor Soj / ParA also targets DnaA filament formation, highlight the critical importance of regulating DnaA helix formation during the initiation reaction. Moreover, these observations lead us to suggest that DnaA oligomerization may be the main regulatory step of the initiator assembly pathway in B . subtilis , in contrast to the prevailing model of bacterial DNA replication based on E scherichia coli DnaA where ATP binding appears to be the targeted activity.