PMID- 10581257
OWN - NLM
STAT- MEDLINE
DCOM- 20000131
LR  - 20161124
IS  - 0261-4189 (Print)
IS  - 1460-2075 (Electronic)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 23
DP  - 1999 Dec 1
TI  - The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is 
      required for the synthesis of multiubiquitin chain.
PG  - 6832-44
AB  - 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.
FAU - Xie, Y
AU  - Xie Y
AD  - Division of Biology, 147-75, California Institute of Technology, 1200 East 
      California Boulevard, Pasadena, CA 91125, USA.
FAU - Varshavsky, A
AU  - Varshavsky A
LA  - eng
GR  - DK39520/DK/NIDDK NIH HHS/United States
GR  - GM31530/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Fungal Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Ubiquitins)
RN  - EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes)
RN  - EC 2.3.2.27 (UBR1 protein, S cerevisiae)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 2.5.1.18 (Glutathione Transferase)
RN  - EC 6.- (Ligases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Fungal Proteins/*chemistry
MH  - Glutathione Transferase/metabolism
MH  - Ligases/*chemistry
MH  - Molecular Sequence Data
MH  - Plasmids/metabolism
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Saccharomyces cerevisiae/chemistry
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
MH  - Signal Transduction
MH  - Two-Hybrid System Techniques
MH  - Ubiquitin-Conjugating Enzymes
MH  - *Ubiquitin-Protein Ligases
MH  - Ubiquitins/*chemistry
PMC - PMC1171746
EDAT- 1999/12/03 00:00
MHDA- 1999/12/03 00:01
CRDT- 1999/12/03 00:00
PHST- 1999/12/03 00:00 [pubmed]
PHST- 1999/12/03 00:01 [medline]
PHST- 1999/12/03 00:00 [entrez]
AID - 10.1093/emboj/18.23.6832 [doi]
PST - ppublish
SO  - EMBO J. 1999 Dec 1;18(23):6832-44. doi: 10.1093/emboj/18.23.6832.