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A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor

Bacteriophage T7 DNA polymerase (gene 5 protein, gp5) interacts with its processivity factor, Escherichia coli thioredoxin, via a unique loop at the tip of the thumb subdomain. We find that this thioredoxin-binding domain is also the site of interaction of the phage-encoded helicase/primase (gp4) an...

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Detaylı Bibliyografya
Asıl Yazarlar: Hamdan, Samir M., Marintcheva, Boriana, Cook, Timothy, Lee, Seung-Joo, Tabor, Stanley, Richardson, Charles C.
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: National Academy of Sciences 2005
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC556000/
https://ncbi.nlm.nih.gov/pubmed/15795374
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0501637102
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