Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us J. Biol. Chem. Oct (2005); 280(43):35822-8 Yeast PIAS-type Ull1-Siz1 is composed of SUMO ligase and regulatory domains- Takahashi Y, Kikuchi Y Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan- Abstract: SUMO -small ubiquitin-like modifier--Smt3 -suppressor of mif two- is a member of the ubiquitin-related protein family and is known to conjugate with many proteins- In the sumoylation pathway, SUMO-Smt3 is transferred to substrate lysine residues through the thioester cascade of E1 -activating enzyme- and E2 -conjugating enzyme-, and E3 -SUMO ligase- functions as an adaptor between E2 and each substrate- Yeast Ull1 -ubiquitin-like protein ligase 1--Siz1, a PIAS -protein inhibitor of activated STAT--type SUMO ligase, modifies both cytoplasmic and nuclear proteins- In this paper, we performed a domain analysis of Ull1-Siz1 by constructing various deletion mutants- A novel conserved N-terminal domain, called PINIT, as well as the RING-like domain -SP-RING- were required for the SUMO ligase activity in the in vitro conjugation system and for interaction with Smt3 in an in vitro binding assay- The most distal N-terminal region, which contains a putative DNA-binding SAF-A-B, Acinus, and PIAS -SAP- motif, was not required for the ligase activity but was involved in nuclear localization- A strong SUMO-binding motif was identified, which interacted with Smt3 in the two-hybrid system but was not necessary for the ligase activity- The most distal C-terminal domain was important for stable localization at the bud neck region and thereby for the substrate recognition of septins- Furthermore, the C-terminal half conferred protein instability on Ull1-Siz1- Taken together, we conclude that the SP-RING and PINIT of Ull1-Siz1 are core domains of the SUMO ligase, and the other domains are regulatory for protein stability and subcellular localization- [PUBMED: 16109721] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.