NDLI: Essential role for ubiquitin–ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate

Content Provider	PubMed Central
Author	Saha, Anjanabha Lewis, Steven Gary, Kleiger Kuhlman, Brian Deshaies, Raymond J.
Copyright Year	2011
Abstract	During ubiquitin conjugation, the thioester bond that links ‘donor’ ubiquitin to ubiquitin-conjugating enzyme (E2) undergoes nucleophilic attack by the ε-amino group of an acceptor lysine, resulting in formation of an isopeptide bond. Models of ubiquitination have envisioned the donor ubiquitin to be a passive participant in this process. However, we show here that the I44A mutation in ubiquitin profoundly inhibits its ability to serve as a donor for ubiquitin chain initiation or elongation, but can be rescued by computationally-predicted compensatory mutations in the E2 Cdc34. The donor defect of ubiquitin-I44A can be partially suppressed either by using a low pKa amine (hydroxylamine) as the acceptor or by performing reactions at higher pH, suggesting that the discharge defect arises in part due to inefficient deprotonation of the acceptor lysine. We propose that interaction between Cdc34 and the donor ubiquitin organizes the active site to promote efficient ubiquitination of substrate.
Related Links	http://dx.doi.org/10.1016/j.molcel.2011.03.016
Ending Page	83
Page Count	9
Starting Page	75
File Format	PDF
ISSN	10972765
e-ISSN	10974164
Journal	Molecular cell
Issue Number	1
Volume Number	42
Language	English
Publisher Date	2011-04-01
Access Restriction	Open
Subject Keyword	Cell Biology Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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