ArticleNucleic acids research2004
A 21-amino acid peptide from the cysteine cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulates its nuclease activity which is Mre11-like and prefers manganese ion as the cofactor.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 29 citations in OpenAlex.
- Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases.Nature communications · 2023Article
- Review
- Two conformations of DNA polymerase D-PCNA-DNA, an archaeal replisome complex, revealed by cryo-electron microscopy.BMC biology · 2020Article
- Elucidating functions of DP1 and DP2 subunits from the Thermococcus kodakarensis family D DNA polymerase.Extremophiles : life under extreme conditions · 2019Article
- Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases.PLoS biology · 2019Article
- Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography.Nature communications · 2016Article
- Pre-steady-state Kinetic Analysis of a Family D DNA Polymerase from Thermococcus sp. 9°N Reveals Mechanisms for Archaeal Genomic Replication and Maintenance.The Journal of biological chemistry · 2015Article
- Characterization of family D DNA polymerase from Thermococcus sp. 9°N.Extremophiles : life under extreme conditions · 2014Article
- Serial intermediates with a 1 nt 3'-flap and 5' variable-length flaps are formed by cooperative functioning of Pyrococcus horikoshii FEN-1 with either B or D DNA polymerases.Extremophiles : life under extreme conditions · 2014Article
- Domain structures and inter-domain interactions defining the holoenzyme architecture of archaeal d-family DNA polymerase.Life (Basel, Switzerland) · 2013Review
- A highly conserved family of inactivated archaeal B family DNA polymerases.Biology direct · 2008Article
- Characterization of the 3' exonuclease subunit DP1 of Methanococcus jannaschii replicative DNA polymerase D.Nucleic acids research · 2004Article
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5 authors at 1 institution in 1 country.
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Abstract
Family D DNA polymerase (PolD) is a new type of DNA polymerase possessing polymerization and 3'-5' exonuclease activities. Here we report the characterization of the nuclease activity of PolD from Pyrococcus horikoshii. By site-directed mutagenesis, we verified that the putative Mre11-like nuclease domain in the small subunit (DP1), predicted according to computer analysis and structure inference reported previously, is the catalytic domain. We show that D363, H365 and H454 are the essential residues, while D407, N453, H500, H563 and H565 are critical residues for the activity. We provide experimental evidence demonstrating that manganese, rather than magnesium, is the preferable metal ion for the nuclease activity of PolD. We also show that DP1 alone is insufficient to perform full catalysis, which additionally requires the formation of the PolD complex and manganese ion. We found that a 21 amino acid, subunit-interacting peptide of the sequence from cysteine cluster II of the large subunit (DP2) stimulates the exonuclease activity of DP1 and the internal deletion mutants of PolD lacking the 21-aa sequence. This indicates that the putative zinc finger motif of the cysteine cluster II is deeply involved in the nucleolytic catalysis.
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