ArticleExtremophiles : life under extreme conditions2007
Biochemical evidence of a physical interaction between Sulfolobus solfataricus B-family and Y-family DNA polymerases.
Article in Extremophiles : life under extreme conditions, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea.Nucleic acids research · 2017Article
- Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity.Biochemistry · 2012Article
- Accurate DNA synthesis by Sulfolobus solfataricus DNA polymerase B1 at high temperature.Extremophiles : life under extreme conditions · 2010Article
- A trimeric DNA polymerase complex increases the native replication processivity.Nucleic acids research · 2009Article
- Inhibition of translesion DNA polymerase by archaeal reverse gyrase.Nucleic acids research · 2009Article
- Archaeal eukaryote-like Orc1/Cdc6 initiators physically interact with DNA polymerase B1 and regulate its functions.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
9 authors.
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Abstract
The hyper-thermophilic archaeon Sulfolobus solfataricus possesses two functional DNA polymerases belonging to the B-family (Sso DNA pol B1) and to the Y-family (Sso DNA pol Y1). Sso DNA pol B1 recognizes the presence of uracil and hypoxanthine in the template strand and stalls synthesis 3-4 bases upstream of this lesion ("read-ahead" function). On the other hand, Sso DNA pol Y1 is able to synthesize across these and other lesions on the template strand. Herein we report evidence that Sso DNA pol B1 physically interacts with DNA pol Y1 by surface plasmon resonance measurements and immuno-precipitation experiments. The region of DNA pol B1 responsible for this interaction has been mapped in the central portion of the polypeptide chain (from the amino acid residue 482 to 617), which includes an extended protease hyper-sensitive linker between the N- and C-terminal modules (amino acid residues Asn482-Ala497) and the alpha-helices forming the "fingers" sub-domain (alpha-helices R, R' and S). These results have important implications for understanding the polymerase-switching mechanism on the damaged template strand during genome replication in S. solfataricus.
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