UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme
Abstract
All known functions of ubiquitin are mediated through its covalent attachment to other proteins. The post‐translational formation of ubiquitin–protein conjugates is preceded by an ATP‐requiring step in which the carboxyl terminus of ubiquitin is adenylated and subsequently joined, through a thiolester bond, to a cysteine residue in the ubiquitin‐activating enzyme, also known as E1. We report the isolation and functional analysis of the gene (UBA1) for the ubiquitin‐activating enzyme of the yeast Saccharomyces cerevisiae. UBA1 encodes a 114 kd protein whose amino acid sequence contains motifs characteristic of nucleotide‐binding sites. Expression of catalytically active UBA1 protein in E. coli, which lacks the ubiquitin system, confirmed that the yeast UBA1 gene encodes a ubiquitin‐activating enzyme. Deletion of the UBA1 gene is lethal, demonstrating that the formation of ubiquitin–protein conjugates is essential for cell viability.
Additional Information
© 1991 European Molecular Biology Organization. Received on September 26, 1990; revised on October 31, 1990. We thank Paul Matsudaira for communicating the PVDF microsequencing procedure prior to publication; Mark Goebl for bringing to our attention the sequence similarity between UBAI and the human AIS9 protein; members of this laboratory for helpful advice, discussion, and comments on the manuscript; and Barbara Doran for secretarial assistance. This work was supported by grants to A.V. from the National Institutes of Health (GM31530 and DK39520). The yeast UBAI sequence will appear in the EMBL, GenBank, and DDBJ nucleotide sequence databases under the accession number X56507.Additional details
- PMCID
- PMC452634
- Eprint ID
- 108000
- DOI
- 10.1002/j.1460-2075.1991.tb07940.x
- Resolver ID
- CaltechAUTHORS:20210210-151525895
- GM31530
- NIH
- DK39520
- NIH
- Created
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2021-02-10Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field