TY - JOUR T1 - Diverse polyubiquitin interaction properties of ubiquitin-associated domains JF - Nature Structural & Molecular Biology Y1 - 2005 A1 - Raasi,Shahri A1 - Varadan,Ranjani A1 - Fushman, David A1 - Pickart,Cecile M. KW - apoptosis KW - basic cellular processes KW - Biochemistry KW - biophysics KW - cell biology KW - cell cycle KW - cell surface proteins KW - cell-cell interactions KW - checkpoints KW - chromatin KW - chromatin remodeling KW - chromatin structure KW - content KW - DNA recombination KW - DNA repair KW - DNA replication KW - Gene expression KW - Genetics KW - intracellular signaling KW - journal KW - macromolecules KW - mechanism KW - membrane processes KW - molecular KW - molecular basis of disease KW - molecular biology KW - molecular interactions KW - multi-component complexes KW - nature publishing group KW - nature structural molecular biology KW - nucleic acids KW - protein degradation KW - protein folding KW - protein processing KW - Proteins KW - regulation of transcription KW - regulation of translation KW - RNA KW - RNA processing KW - RNAi KW - signal transduction KW - single molecule studies KW - structure and function of proteins KW - transcription KW - translation AB - The ubiquitin-associated (UBA) domain occurs frequently in proteins involved in ubiquitin-dependent signaling pathways. Although polyubiquitin chain binding is considered to be a defining feature of the UBA domain family, the generality of this property has not been established. Here we have surveyed the polyubiquitin interaction properties of 30 UBA domains, including 16 of 17 occurrences in budding yeast. The UBA domains sort into four classes that include linkage-selective polyubiquitin binders and domains that bind different chains (and monoubiquitin) in a nondiscriminatory manner; one notable class (30%) did not bind any ubiquitin ligand surveyed. The properties of a given UBA domain are conserved from yeast to mammals. Their functional relevance is further suggested by the ability of an ectopic UBA domain to alter the specificity of a deubiquitylating enzyme in a predictable manner. Conversely, non-UBA sequences can modulate the interaction properties of a UBA domain. VL - 12 SN - 1545-9993 UR - http://www.nature.com/nsmb/journal/v12/n8/full/nsmb962.html CP - 8 M3 - 10.1038/nsmb962 ER -