The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex.

@article{Kobori1982TheEC,
  title={The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex.},
  author={Joan A. Kobori and Arthur Kornberg},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 22},
  pages={13770-5}
}
The Escherichia coli dnaB and dnaC proteins form a tight complex in the presence of ATP (Wickner, S., and Hurwitz, J., (1975) Proc. Natl. Acad. Sci. U. S. A. 72, 921-925). The complexed dnaC protein is resistant to inhibition by the sulfhydryl reagent, N-ethylmaleimide. This protection is not observed when ATP is substituted by AMP, ADP, adenyl 5'-yl imidodiphosphate, or adenosine-5'-O-(3-thiotriphosphate); dATP provides partial protection. A sedimentation coefficient of 15.2 S determined by… CONTINUE READING