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The E2–E3 interaction in the N‐end rule pathway: the RING‐H2 finger of E3 is required for the synthesis of multiubiquitin chain

The E2–E3 interaction in the N‐end rule pathway: the RING‐H2 finger of E3 is required for the... We dissected physical and functional interactions between the ubiquitin‐conjugating (E2) enzyme Ubc2p and Ubr1p, the E3 component of the N‐end rule pathway in Saccharomyces cerevisiae. The binding of the 20 kDa Ubc2p by the 225 kDa Ubr1p is shown to be mediated largely by the basic residue‐rich (BRR) region of Ubr1p. However, mutations of the BRR domain that strongly decrease the interaction between Ubr1p and Ubc2p do not prevent the degradation of N‐end rule substrates. In contrast, this degradation is completely dependent on the RING‐H2 finger of Ubr1p adjacent to the BRR domain. Specifically, the first cysteine of RING‐H2 is required for the ubiquitylation activity of the Ubr1p–Ubc2p complex, although this cysteine plays no detectable role in either the binding of N‐end rule substrates by Ubr1p or the physical affinity between Ubr1p and Ubc2p. These results defined the topography of the Ubc2p–Ubr1p interaction and revealed the essential function of the RING‐H2 finger, a domain that is present in many otherwise dissimilar E3 proteins of the ubiquitin system. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

The E2–E3 interaction in the N‐end rule pathway: the RING‐H2 finger of E3 is required for the synthesis of multiubiquitin chain

The EMBO Journal , Volume 18 (23) – Jan 1, 1999

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References (91)

Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1093/emboj/18.23.6832
pmid
10581257
Publisher site
See Article on Publisher Site

Abstract

We dissected physical and functional interactions between the ubiquitin‐conjugating (E2) enzyme Ubc2p and Ubr1p, the E3 component of the N‐end rule pathway in Saccharomyces cerevisiae. The binding of the 20 kDa Ubc2p by the 225 kDa Ubr1p is shown to be mediated largely by the basic residue‐rich (BRR) region of Ubr1p. However, mutations of the BRR domain that strongly decrease the interaction between Ubr1p and Ubc2p do not prevent the degradation of N‐end rule substrates. In contrast, this degradation is completely dependent on the RING‐H2 finger of Ubr1p adjacent to the BRR domain. Specifically, the first cysteine of RING‐H2 is required for the ubiquitylation activity of the Ubr1p–Ubc2p complex, although this cysteine plays no detectable role in either the binding of N‐end rule substrates by Ubr1p or the physical affinity between Ubr1p and Ubc2p. These results defined the topography of the Ubc2p–Ubr1p interaction and revealed the essential function of the RING‐H2 finger, a domain that is present in many otherwise dissimilar E3 proteins of the ubiquitin system.

Journal

The EMBO JournalWiley

Published: Jan 1, 1999

Keywords: ; ; ; ; ;

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