The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme
Abstract
Mutants in the gene CDC34 of the yeast Saccharomyces cerevisiae are defective in the transition from G1 to the S phase of the cell cycle. This gene was cloned and shown to encode a 295-residue protein that has substantial sequence similarity to the product of the yeast RAD6 gene. The RAD6 gene is required for a variety of cellular functions including DNA repair and was recently shown to encode a ubiquitin-conjugating enzyme. When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes. The cell cycle function of CDC34 is thus likely to be mediated by the ubiquitin-conjugating activity of its product.
Additional Information
© 1988 American Association for the Advancement of Science. 9 March 1988; accepted 29 June 1988. We thank L. Hartweli, W. Fangman, A. Hopper, J. Hurley, D. Finley, and B. Bartel for advice during the preparation of the manuscript. We thank C. Mann for the gift of plasmid CMp170 and R. McCarroll for the Southern blot of separated yeast chromosomes. Supported by grants from the National Institute of General Medical Sciences to B.B. (GM18541) and A.V. (GM31530).Additional details
- Eprint ID
- 107825
- DOI
- 10.1126/science.2842867
- Resolver ID
- CaltechAUTHORS:20210129-142403433
- GM18541
- NIH
- GM31530
- NIH
- Created
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2021-02-01Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field