ArticleJournal of bacteriology2005
The bacteriophage P1 hot gene product can substitute for the Escherichia coli DNA polymerase III {theta} subunit.
Article in Journal of bacteriology, 2005. 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, 20 citations in OpenAlex.
- Identification, Characterization, and Genomic Analysis of NovelInternational journal of molecular sciences · 2020Article
- Computational Simulations of DNA Polymerases: Detailed Insights on Structure/Function/Mechanism from Native Proteins to Cancer Variants.Chemical research in toxicology · 2017Article
- When Competing Viruses Unify: Evolution, Conservation, and Plasticity of Genetic Identities.Journal of molecular evolution · 2015Article
- Evidence for moonlighting functions of the θ subunit of Escherichia coli DNA polymerase III.Journal of bacteriology · 2014Article
- DNA replication fidelity in Escherichia coli: a multi-DNA polymerase affair.FEMS microbiology reviews · 2012Review
- Stabilization of the Escherichia coli DNA polymerase III ε subunit by the θ subunit favors in vivo assembly of the Pol III catalytic core.Archives of biochemistry and biophysics · 2012Article
- High-throughput comparison of gene fitness among related bacteria.BMC genomics · 2012Article
- dnaX36 Mutator of Escherichia coli: effects of the {tau} subunit of the DNA polymerase III holoenzyme on chromosomal DNA replication fidelity.Journal of bacteriology · 2011Article
- Mutators and hypermutability in bacteria: the Escherichia coli paradigm.Journal of genetics · 2009Review
- Reaction mechanism of the epsilon subunit of E. coli DNA polymerase III: insights into active site metal coordination and catalytically significant residues.Journal of the American Chemical Society · 2009Article
- The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker.Nucleic acids research · 2008Article
- The bacteriophage P1 hot gene, encoding a homolog of the E. coli DNA polymerase III theta subunit, is expressed during both lysogenic and lytic growth stages.Mutation research · 2007Article
- Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex.The Journal of biological chemistry · 2006Article
- Mutator and antimutator effects of the bacteriophage P1 hot gene product.Journal of bacteriology · 2006Article
- Structure of the theta subunit of Escherichia coli DNA polymerase III in complex with the epsilon subunit.Journal of bacteriology · 2006Article
- Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit.Journal of bacteriology · 2005Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
The theta subunit (holE gene product) of Escherichia coli DNA polymerase (Pol) III holoenzyme is a tightly bound component of the polymerase core. Within the core (alpha-epsilon-theta), the alpha and epsilon subunits carry the DNA polymerase and 3' proofreading functions, respectively, while the precise function of theta is unclear. holE homologs are present in genomes of other enterobacteriae, suggestive of a conserved function. Putative homologs have also been found in the genomes of bacteriophage P1 and of certain conjugative plasmids. The presence of these homologs is of interest, because these genomes are fully dependent on the host replication machinery and contribute few, if any, replication factors themselves. To study the role of these theta homologs, we have constructed an E. coli strain in which holE is replaced by the P1 homolog, hot. We show that hot is capable of substituting for holE when it is assayed for its antimutagenic action on the proofreading-impaired dnaQ49 mutator, which carries a temperature-sensitive epsilon subunit. The ability of hot to substitute for holE was also observed with other, although not all, dnaQ mutator alleles tested. The data suggest that the P1 hot gene product can substitute for the theta subunit and is likely incorporated in the Pol III complex. We also show that overexpression of either theta or Hot further suppresses the dnaQ49 mutator phenotype. This suggests that the complexing of dnaQ49-epsilon with theta is rate limiting for its ability to proofread DNA replication errors. The possible role of hot for bacteriophage P1 is discussed.
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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.