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A novel protein modification pathway related to the ubiquitin system.

The EMBO journal | Apr 15, 1998

http://www.ncbi.nlm.nih.gov/pubmed/9545234

Ubiquitin conjugation is known to target protein substrates primarily to degradation by the proteasome or via the endocytic route. Here we describe a novel protein modification pathway in yeast which mediates the conjugation of RUB1, a ubiquitin-like protein displaying 53% amino acid identity to ubiquitin. We show that RUB1 conjugation requires at least three proteins in vivo. ULA1 and UBA3 are related to the N- and C-terminal domains of the E1 ubiquitin-activating enzyme, respectively, and together fulfil E1-like functions for RUB1 activation. RUB1 conjugation also requires UBC12, a protein related to E2 ubiquitin-conjugating enzymes, which functions analogously to E2 enzymes in RUB1-protein conjugate formation. Conjugation of RUB1 is not essential for normal cell growth and appears to be selective for a small set of substrates. Remarkably, CDC53/cullin, a common subunit of the multifunctional SCF ubiquitin ligase, was found to be a major substrate for RUB1 conjugation. This suggests that the RUB1 conjugation pathway is functionally affiliated to the ubiquitin-proteasome system and may play a regulatory role.

Pubmed ID: 9545234 RIS Download

Mesh terms: Amino Acid Sequence | Base Sequence | Cell Cycle Proteins | Cullin Proteins | DNA, Complementary | Fungal Proteins | Ligases | Molecular Sequence Data | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Sequence Homology, Amino Acid | Substrate Specificity | Ubiquitin-Activating Enzymes | Ubiquitin-Conjugating Enzymes | Ubiquitin-Protein Ligases | Ubiquitins

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