Diverse polyubiquitin interaction properties of ubiquitin-associated domains - PubMed (original) (raw)
Comparative Study
doi: 10.1038/nsmb962. Epub 2005 Jul 10.
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- PMID: 16007098
- DOI: 10.1038/nsmb962
Comparative Study
Diverse polyubiquitin interaction properties of ubiquitin-associated domains
Shahri Raasi et al. Nat Struct Mol Biol. 2005 Aug.
Abstract
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 ( approximately 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.
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