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J. Biol. Chem., Vol. 261, Issue 25, 11460-11465, 09, 1986
KO Johanson, TE Haynes and CS McHenry
We have purified the beta subunit of the DNA polymerase III holoenzyme to
homogeneity from an overproducing strain (Blanar, M., Sandler, S.,
Armengod, M., Ream, L., and Clark, A. (1984) Proc. Natl. Acad. Sci. U.S.A.
81, 4622-4626). From this procedure we can obtain 100 mg quantities of
protein. The beta isolated from the overproducer is indistinguishable from
that isolated from wild-type cells in terms of its activity and molecular
weight. Partial amino acid sequence analysis has confirmed the DNA sequence
of the dnaN gene (Ohmori, H., Kimura, M., Nagata, T., and Sakakibara, Y.
(1984) Gene (Amst.) 28, 159-170) and established the sites for initiation
and termination of translation. No processing that removes amino acid
residues from beta occurs since the active protein begins with the
initiating methionine and terminates at the position predicted from the DNA
sequence. Our knowledge of the precise amino acid composition has been used
to determine the extinction coefficient of beta to be 17,900 and 18,700
cm-1 M-1 at 280 and 277 nm, respectively. The extinction coefficient at 280
nm is reduced to 14,700 cm-1 M-1 under denaturing conditions in guanidine
HCl. Conditions have been optimized so that 1 N-ethylmaleimide residue can
be incorporated per beta monomer with full preservation of activity.
Chemical characterization and purification of the beta subunit of the DNA polymerase III holoenzyme from an overproducing strain
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