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Nucleic Acids Research, 1987, Vol. 15, No. 19 7663-7675
© 1987

Articles

Relation of the Escherichia coli dnaX gene to its two products-the {tau} and {gamma} subunits of DNA polymerase III holoenzyme

Suk-Hee Lee, Patrick Kanda1, Ronald C. Kennedy1 and James R. Walker

Department of Microbiology, University of Texas Austin, TX 78712, USA 1Department of Virology and Immunology, Southwest Foundation for Biomedical Research San Antonio, TX 78284, USA

Received June 10, 1987. Accepted September 1, 1987.

The Escherichia coli DNA polymerase III holoenzyme 71.1 kDa {tau} subunit is a 643 amino acid protein encoded by the dnaX gene. This gene also encodes the holoenzyme 56.5 kDa {gamma} subunit. The {tau} factor (as a {tau}' -LacZ' fusion protein) has been isolated and shown to be cleaved in vitro to form {gamma} and a 135 kda C-terminal cleavage product. The {tau}' -LacZ' fusion protein, {gamma}, and the C-terminal cleavage product have been isolated. N-terminal sequencing has demonstrated that {tau} and {gamma} share the same N-terminal sequences and that {tau} is proteolytically cleaved in vitro between residues 498 and 499 to form {gamma}. In addition, residues 420–440 were shown to be present in both {tau} and {gamma} by use of antibody specific for a synthetic peptide corresponding to that sequence. Some mechanism functions in vivo to ensure that {tau} and {gamma} are synthesized in a ratio of about one-to-one, as shown by radioimmune precipitation of {tau} and {gamma} from cellular extracts.


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