Nucleic Acids Research, Vol 26, Issue 2 477-485, Copyright © 1998 by Oxford University Press
K Hashimoto, N Nakashima, T Ohara, S Maki and A Sugino
DNA polymerase III (delta) of Saccharomyces cerevisiae is purified as a
complex of at least two polypeptides with molecular masses of 125 and 55
kDa as judged by SDS-PAGE. In this paper we determine partial amino acid
sequences of the 125 and 55 kDa polypeptides and find that they match parts
of the amino acid sequences predicted from the nucleotide sequence of the
CDC2 and HYS2 genes respectively. We also show by Western blotting that
Hys2 protein co-purifies with DNA polymerase III activity as well as Cdc2
polypeptide. The complex form of DNA polymerase III activity could not be
detected in thermosensitive hys2 mutant cell extracts, although another
form of DNA polymerase III was found. This form of DNA polymerase III,
which could also be detected in wild-type extracts, was not associated with
Hys2 protein and was not stimulated by addition of proliferating cell
nuclear antigen (PCNA), replication factor A (RF-A) or replication factor C
(RF-C). The temperature-sensitive growth phenotype of hys2-1 and hys2-2
mutations could be suppressed by the CDC2 gene on a multicopy plasmid.
These data suggest that the 55 kDa polypeptide encoded by the HYS2 gene is
one of the subunits of DNA polymerase III complex in S.cerevisiae and is
required for highly processive DNA synthesis catalyzed by DNA polymerase
III in the presence of PCNA, RF-A and RF-C.
ARTICLES
The second subunit of DNA polymerase III (delta) is encoded by the HYS2 gene in Saccharomyces cerevisiae
Department of Biochemistry and Molecular Biology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-Oka, Suita, Osaka 565, Japan.
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