Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III.

@article{DeRose2004PhageLI,
  title={Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III.},
  author={Eugene F. DeRose and Thomas W Kirby and Geoffrey A. Mueller and Anna K. Chikova and Roel M. Schaaper and Robert E. London},
  journal={Structure},
  year={2004},
  volume={12 12},
  pages={2221-31}
}
DNA polymerase III, the main replicative polymerase of E. coli, contains a small subunit, theta, that binds to the epsilon proofreading subunit and appears to enhance the enzyme's proofreading function--especially under extreme conditions. It was recently discovered that E. coli bacteriophage P1 encodes a theta homolog, named HOT. The (1)H-(15)N HSQC spectrum of HOT exhibits more uniform intensities and less evidence of conformational exchange than that of theta; this uniformity facilitates a… CONTINUE READING

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