Nucleic Acids Research, Vol 27, Issue 4 993-1000, Copyright © 1999 by Oxford University Press
SW Ng, Y Liu, KT Hasselblatt, SC Mok and RS Berkowitz
Eukaryotic DNA topoisomerase III was first identified by studying the
hyper-recombination and slow growth phenotypes of yeast mutants.
Topoisomerase III interacts with DNA helicase SGS1 and the two proteins are
involved in DNA recombination, cellular aging and maintenance of genome
stability. A human homolog of topoisomerase III has previously been
identified. Here we report the identification of cDNAs and the
determination of gene structure for a second human topoisomerase III gene.
This novel gene expresses three alternatively spliced transcripts, which
encode gene products different in the putative DNA- binding C-termini. The
largest gene product of the novel topoisomerase III was expressed and shown
to interact with SGS1 protein and partially rescue the slow growth defect
of a yeast topoisomerase III mutant. The presence of more than one human
topoisomerase III is reminiscent of mammalian topoisomerase II, which has
two genetically distinct isoforms with different expression patterns and
probably different functions in mammalian cells.
ARTICLES
A new human topoisomerase III that interacts with SGS1 protein
Laboratory of Gynecologic Oncology, Department of Obstetrics, Gynecology and Reproductive Biology,Brigham and Women's Hospital, 221 Longwood Avenue, Boston, MA 02115, USA. sgn@rics.bwh.harvard.edu
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