UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme.
AUTOR(ES)
McGrath, J P
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=452634Documentos Relacionados
- Phosphorylation of ubiquitin-activating enzyme in cultured cells.
- Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1.
- Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1.
- Association of ubiquitin-activating enzyme with HeLa cell chromosomes during mitosis.
- Immunoelectron microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells.