ArticleNucleic acids research2007
Mechanism for the TtDnaA-Tt-oriC cooperative interaction at high temperature and duplex opening at an unusual AT-rich region in Thermoanaerobacter tengcongensis.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 11 citations in OpenAlex.
- Robust helicase loading mechanism underlies diverse architectures of bacterial replication origins.Nucleic acids research · 2026Article
- The bacterial DnaA-trio replication origin element specifies single-stranded DNA initiator binding.Nature · 2016Article
- Initiation of Chromosomal Replication in Predatory BacteriumFrontiers in microbiology · 2016Article
- Choosing a suitable method for the identification of replication origins in microbial genomes.Frontiers in microbiology · 2015Review
- Highly organized DnaA-oriC complexes recruit the single-stranded DNA for replication initiation.Nucleic acids research · 2012Article
- Two distantly homologous DnaG primases from Thermoanaerobacter tengcongensis exhibit distinct initiation specificities and priming activities.Journal of bacteriology · 2010Article
- Characterization of EndoTT, a novel single-stranded DNA-specific endonuclease from Thermoanaerobacter tengcongensis.Nucleic acids research · 2010Article
- Multiple replication origins of Halobacterium sp. strain NRC-1: properties of the conserved orc7-dependent oriC1.Journal of bacteriology · 2009Article
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6 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Thermoanaerobacter tengcongensis is an anaerobic low-GC thermophilic bacterium. To further elucidate the replication initiation of chromosomal DNA at high temperature, the interaction between the replication initiator (TtDnaA) and the putative origin (Tt-oriC) in this thermophile was investigated. We found that efficient binding of TtDnaA to Tt-oriC at high temperature requires (i) at least two neighboring DnaA boxes, (ii) the specific feature of the TtDnaA Domain IV and (iii) the self-oligomerization of TtDnaA. Replacement of the TtDnaA Domain IV by the counterpart of Escherichia coli DnaA or disruption of its oligomerization by amino acid mutations (W9A/L20S) abolished the oriC-binding activity of TtDnaA at 60 degrees C, but not at 37 degrees C. Moreover, ATP-TtDnaA, but not ADP-TtDnaA or the oligomerization-deficient mutants was able to unwind the Tt-oriC duplex. The minimal oriC required for this duplex opening in vitro was demonstrated to consist of DnaA boxes 1-8 and an unusual AT-rich region. Interestingly, although no typical ATP-DnaA box was found in this AT-rich region, it was exclusively bound by ATP-TtDnaA and acted as the duplex-opening and replication-initiation site. Taken together, we propose that oligomerization of ATP-DnaA and simultaneously binding of several DnaA boxes and/or AT-rich region may be generally required in replication initiation at high temperature.
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