Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 14, Pages 5096-5101Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0501637102
Keywords
DNA replication; molecular switch; replisome; gene 4 protein; thioredoxin
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Funding
- NIGMS NIH HHS [F32GM72305, R01 GM054397, F32 GM072305, GM-54397] Funding Source: Medline
- OHS HRSA HHS [ST32A107245-20] Funding Source: Medline
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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) and ssDNA binding protein (gp2.5). Thioredoxin itself interacts only weakly with gp4 and gp2.5 but drastically enhances their binding to gp5. The acidic C termini of gp4 and gp2.5 are critical for this interaction in the absence of DNA. However, the C-terminal tail of gp4 is not required for binding to gp5 when the latter is bound to a primer/template. We propose that the thioredoxin-binding domain is a molecular switch that regulates the interaction of T7 DNA polymerase with other proteins of the replisome.
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