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PMID:2209542
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| Citation |
Bartel, B, Wünning, I and Varshavsky, A (1990) The recognition component of the N-end rule pathway. EMBO J. 9:3179-89 |
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| Abstract |
The N-end rule-based degradation signal, which targets a protein for ubiquitin-dependent proteolysis, comprises a destabilizing amino-terminal residue and a specific internal lysine residue. We report the isolation and functional analysis of a gene (UBR1) for the N-end recognizing protein of the yeast Saccharomyces cerevisiae. UBR1 encodes a approximately 225 kd protein with no significant sequence similarities to other known proteins. Null ubr1 mutants are viable but are unable to degrade the substrates of the N-end rule pathway. These mutants are partially defective in sporulation and grow slightly more slowly than their wild-type counterparts. The UBR1 protein specifically binds in vitro to proteins bearing amino-terminal residues that are destabilizing according to the N-end rule, but does not bind to otherwise identical proteins bearing stabilizing amino-terminal residues. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA, Fungal/genetics; DNA, Fungal/isolation & purification; Fungal Proteins/genetics; Fungal Proteins/metabolism; Genes, Fungal; Genotype; Ligases; Molecular Sequence Data; Mutation; Oligonucleotide Probes; Phenotype; Plasmids; Restriction Mapping; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/growth & development; Saccharomyces cerevisiae Proteins; Substrate Specificity; Ubiquitin-Protein Ligases |
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