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PMID: 16338353 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Identification and characterization of modular domains that bind ubiquitin.

Methods in enzymology ·Vol. 399 ·2005-00-00 ·Pages 135-57

French M, Swanson K, Shih SC, Radhakrishnan I, Hicke L

Abstract

To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.

MeSH Terms
Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Models, Molecular Nuclear Magnetic Resonance, Biomolecular Protein Conformation Two-Hybrid System Techniques Ubiquitin/chemistry,metabolism
Chemicals
Ubiquitin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
French Michael
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois, USA.
Swanson Kurt
Shih Susan C
Radhakrishnan Ishwar
Hicke Linda
Article Info
Journal
Methods in enzymology
Abbr.
Methods Enzymol
ISSN
0076-6879
Published
2005-00-00
Pages
135-57
Language
English
Region
United States
NLM ID
0212271
Subset
IM
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