Volume 271, Number 52, Issue of December 27, 1996 pp. 33678-33685
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of a High Mobility Group 1/2 Homolog in Yeast

(Received for publication, August 9, 1996, and in revised form, September 9, 1996)

Jian Lu , Ryuji Kobayashi ^§ and Steven J. Brill

From the  Department of Molecular Biology and Biochemistry, Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08855 and the ^§ Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724

A 35-kDa polypeptide belonging to the high mobility group family of proteins was purified from the yeast Saccharomyces cerevisiae on the basis of its association with a DNA helicase activity. Amino acid sequence alignment suggests that this protein, Hmo1p, is related to the HMG1/2 class of chromatin-associated proteins. Consistent with this prediction, the Hmo1 protein immunolocalizes to the nucleus, binds single-stranded DNA, and unwinds DNA in the presence of eukaryotic DNA topoisomerase I. While the purified protein has no DNA helicase activity on its own, immunoprecipitation experiments confirm that Hmo1p associates with a 5 to 3 DNA helicase activity in nuclear extracts. The in vivo role of the protein was investigated by constructing an hmo1 deletion mutant. This strain has a severe growth defect, reduced plasmid stability, and chromatin that is hypersensitive to micrococcal nuclease digestion. Taken together, the data indicate that HMO1 is likely to be the homolog of HMG1/2 in higher cells and that it plays an important role in genome maintenance.

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