Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Quick Search
My eDoc
Session History
Support Wiki
Direct access to
document ID:

          Institute: MPI für Biochemie     Collection: Molecular Cell Biology (S. Jentsch)     Display Documents

ID: 41777.0, MPI für Biochemie / Molecular Cell Biology (S. Jentsch)
Interaction of the developmental regulator SALL1 with UBE2I and SUMO-1
Authors:Netzer, C.; Bohlander, S. K.; Rieger, L.; Muller, S.; Kohlhase, J.
Date of Publication (YYYY-MM-DD):2002-08-30
Title of Journal:Biochemical and Biophysical Research Communications
Journal Abbrev.:Biochem. Biophys. Res. Commun.
Issue / Number:4
Start Page:870
End Page:876
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Mutations in the SALL1 gene on chromosome 16q12.1 cause Townes- Brocks syndrome (TBS). This autosomal dominantly inherited disorder is characterized by typical malformations of the thumbs, the ears, and the anus, and also commonly affects the kidneys and other organ systems. SALL1 has recently been shown to localize to chromocenters and other heterochromatin foci in murine fibroblasts and to interact with the telomere-repeat- binding factor TRF1/PIN2. Here, we show that the ubiquitin- conjugating enzyme 21 (UBE2I), the human homolog of S. cerevisiae UBC9, and the small ubiquitin-like modifier-1 (SUMO- 1) interact with SALL1 in the yeast two-hybrid system. The interaction of SALL1 and UBE21 was confirmed in a glutathione S-transferase (GST) pull-down experiment. In an in vitro assay, it could be demonstrated that SALL1 is covalently modified by at least two SUMO-1 molecules in the presence of UBA2/AOS1 and UBE21. Mutation of lysine 1086 of SALL1 to arginine abrogates SALL1 sumoylation, suggesting the presence of a polymeric SUMO- I chain in the wild type state. (C) 2002 Elsevier Science (USA). All rights reserved.
Free Keywords:SALL1; UBE2I; SUMO-1; Townes-Brocks syndrome; protein-protein interaction
Comment of the Author/Creator:Date: 2002, AUG 30
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Molecular Cell Biology (S. Jentsch)/Research Group S. Müller
External Affiliations:Univ Munich, Dept Med 2, Marchioninistr 25, D-81377 Munich,; Germany; GSF, Clin Cooperat Grp Leukemia, D-81377 Munich, Germany; Univ Gottingen, Inst Human Genet, D-37073 Gottingen, Germany
Identifiers:ISI:000180887000014 [ID No:1]
ISSN:0006-291X [ID No:2]
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.