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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...
Tallennettuna:
| Päätekijät: | , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
2005
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| Aiheet: | |
| Linkit: | 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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