ArticleThe Journal of biological chemistry2011
DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- DNA replication initiation timing is important for maintaining genome integrity.Journal of bacteriology · 2025Article
- Negative feedback for DARS2-Fis complex by ATP-DnaA supports the cell cycle-coordinated regulation for chromosome replication.Nucleic acids research · 2021Article
- HdaB: a novel and conserved DnaA-related protein that targets the RIDA process to stimulate replication initiation.Nucleic acids research · 2020Article
- Persistence of Intracellular Bacterial Pathogens-With a Focus on the Metabolic Perspective.Frontiers in cellular and infection microbiology · 2020Review
- Fundamental principles in bacterial physiology-history, recent progress, and the future with focus on cell size control: a review.Reports on progress in physics. Physical Society (Great Britain) · 2018Review
- The DnaA Tale.Frontiers in microbiology · 2018Review
- Review
- Dynamic assembly of Hda and the sliding clamp in the regulation of replication licensing.Nucleic acids research · 2017Article
- Review
- The DnaA Cycle inFrontiers in microbiology · 2017Review
- The orisome: structure and function.Frontiers in microbiology · 2015Review
- Mutant DnaAs of Escherichia coli that are refractory to negative control.Nucleic acids research · 2013Article
- Crosstalk between DnaA protein, the initiator of Escherichia coli chromosomal replication, and acidic phospholipids present in bacterial membranes.International journal of molecular sciences · 2013Review
- Regulating DNA replication in bacteria.Cold Spring Harbor perspectives in biology · 2013Review
- Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complex.The Journal of biological chemistry · 2012Article
- Evidence for roles of the Escherichia coli Hda protein beyond regulatory inactivation of DnaA.Molecular microbiology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chromosomal replication is initiated from the replication origin oriC in Escherichia coli by the active ATP-bound form of DnaA protein. The regulatory inactivation of DnaA (RIDA) system, a complex of the ADP-bound Hda and the DNA-loaded replicase clamp, represses extra initiations by facilitating DnaA-bound ATP hydrolysis, yielding the inactive ADP-bound form of DnaA. However, the mechanisms involved in promoting the DnaA-Hda interaction have not been determined except for the involvement of an interaction between the AAA+ domains of the two. This study revealed that DnaA Leu-422 and Pro-423 residues within DnaA domain IV, including a typical DNA-binding HTH motif, are specifically required for RIDA-dependent ATP hydrolysis in vitro and that these residues support efficient interaction with the DNA-loaded clamp·Hda complex and with Hda in vitro. Consistently, substitutions of these residues caused accumulation of ATP-bound DnaA in vivo and oriC-dependent inhibition of cell growth. Leu-422 plays a more important role in these activities than Pro-423. By contrast, neither of these residues is crucial for DNA replication from oriC, although they are highly conserved in DnaA orthologues. Structural analysis of a DnaA·Hda complex model suggested that these residues make contact with residues in the vicinity of the Hda AAA+ sensor I that participates in formation of a nucleotide-interacting surface. Together, the results show that functional DnaA-Hda interactions require a second interaction site within DnaA domain IV in addition to the AAA+ domain and suggest that these interactions are crucial for the formation of RIDA complexes that are active for DnaA-ATP hydrolysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.