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PMID:1651502

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Citation

Dohmen, RJ, Madura, K, Bartel, B and Varshavsky, A (1991) The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme. Proc. Natl. Acad. Sci. U.S.A. 88:7351-5

Abstract

The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all organisms examined, from mammals to bacteria. We show that UBC2(RAD6), one of at least seven ubiquitin-conjugating enzymes in the yeast Saccharomyces cerevisiae, is essential for multiubiquitination and degradation of the N-end rule substrates. We also show that UBC2 is physically associated with UBR1, the recognition component of the N-end rule pathway. These results indicate that some of the UBC2 functions, which include DNA repair, induced mutagenesis, sporulation, and regulation of retrotransposition, are mediated by protein degradation via the N-end rule pathway.

Links

PubMed PMC52293

Keywords

DNA Repair; Fungal Proteins/metabolism; Haploidy; Ligases/genetics; Ligases/metabolism; Models, Biological; Protein Binding; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae Proteins; Ubiquitin-Conjugating Enzymes; Ubiquitins/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

YEAST:UBC2

involved_in

GO:0071596: ubiquitin-dependent protein catabolic process via the N-end rule pathway

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:UBC2

involved_in

GO:0000209: protein polyubiquitination

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

YEAST:UBC2

part_of

GO:1990303: UBR1-RAD6 ubiquitin ligase complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P19812

C

Seeded From UniProt

complete

YEAST:UBC2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P19812

F

Seeded From UniProt

complete

YEAST:UBR1

part_of

GO:1990303: UBR1-RAD6 ubiquitin ligase complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P06104

C

Seeded From UniProt

complete

YEAST:UBR1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P06104

F

Seeded From UniProt

complete


See also

References

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