Document Detail

Identification of molecular determinants required for interaction of ubiquitin-conjugating enzymes and RING finger proteins.
MedLine Citation:
PMID:  11722579     Owner:  NLM     Status:  MEDLINE    
Recent results from several laboratories suggest that the interaction of E2 ubiquitin-conjugating enzymes with the RING finger domain has a central role in mediating the transfer of ubiquitin to proteins. Here we present a mutational analysis of the interaction between the E2 enzyme UbcM4/UbcH7 and three different RING finger proteins, termed UIPs, which, like Parkin, contain a RING1-IBR-RING2 motif. The results show that the E2 enzyme binds to the RING1 domain but not to the other cysteine/histidine-rich domains of the RING1-IBR-RING2 motif. Three regions within the UbcM4 molecule are involved in this interaction: the H1 alpha helix, loop L1, connecting the third and fourth strand of the beta sheet, and loop L2, located between the fourth beta strand and the second alpha helix. Loop L2 plays an important role in determining the specificity of interaction. The effects of L2 mutations on UbcM4/UIP interaction are different for each UIP, indicating that RING finger domains can vary considerably in their structural requirements for binding to E2 enzymes. The result that single amino-acid changes can regulate binding of E2 enzymes to different RING finger proteins suggests a novel approach to experimentally manipulate proteolytic pathways mediated by RING finger proteins.
G Martinez-Noel; U Müller; K Harbers
Related Documents :
21300909 - P31comet promotes disassembly of the mitotic checkpoint complex in an atp-dependent pro...
22120669 - Probing the specificity of gamma-glutamylamine cyclotransferase: an enzyme involved in ...
18997779 - Structure of a shigella effector reveals a new class of ubiquitin ligases.
20399179 - And yet it moves: active site remodeling in the sumo e1.
19945379 - Rapid e2-e3 assembly and disassembly enable processive ubiquitylation of cullin-ring ub...
16551269 - Tyk2 activity promotes ligand-induced ifnar1 proteolysis.
19053249 - Structural studies of interactions between cardiac troponin i and actin in regulated th...
2644279 - Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by my...
22781759 - The yeast regulator of transcription protein rtr1 lacks an active site and phosphatase ...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  268     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-11-27     Completed Date:  2001-12-31     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  5912-9     Citation Subset:  IM    
Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, Hamburg, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
DNA-Binding Proteins / chemistry,  genetics,  metabolism*
Ligases / chemistry,  genetics,  metabolism*
Molecular Sequence Data
Protein Binding
Sequence Homology, Amino Acid
Ubiquitin / metabolism*
Ubiquitin-Conjugating Enzymes
Zinc Fingers
Reg. No./Substance:
0/DNA-Binding Proteins; 0/Ubiquitin; EC 6.-/Ligases; EC Enzymes

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Molecular mechanism for osmolyte protection of creatine kinase against guanidine denaturation.
Next Document:  Cyclic AMP regulates expression of the RI alpha subunit of cAMP-dependent protein kinase through an ...