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- Title
60th residues of ubiquitin and Nedd8 are located out of E2-binding surfaces, but are important for K48 ubiquitin-linkage
- Authors
Choi, Yun-Seok; Jeon, Young Ho; Ryu, Kyoung-Seok; Cheong, Chaejoon
- Abstract
Abstract: Nedd8, a ubiquitin-like modifier, is covalently attached to various proteins. Although Nedd8 has higher sequence identity (57%) with ubiquitin, its conserved K48 residue cannot form covalent linkage with ubiquitin. To decipher the reason why Nedd8 cannot be an effective ubiquitin-acceptor, we compared the non-covalent interaction between Nedd8 and ubiquitin for various E2s using cross-saturation NMR technique. However, both Nedd8 and ubiquitin displayed almost identical non-covalent E2-binding properties. The K60 of Nedd8 was not present at the E2-binding surface, but its mutation to Asn converted Nedd8 into a ubiquitin-acceptor. The N60 ubiquitin mutants also displayed a decreased ubiquitin-accepting activity. These results suggest the presence of an uncharacterized determinant for the K48 ubiquitin-linkage that is not related to non-covalent E2-bindings. Structured summary: MINT-7263328: NEDD8 (uniprotkb:Q15843) and Ubiquitin (uniprotkb:P62988) physically interact (MI:0914) by enzymatic studies (MI:0415)
- Subjects
UBIQUITIN; BINDING sites; AMINO acid sequence; GENETIC mutation; PROTEIN-protein interactions; COMPARATIVE studies
- Publication
FEBS Letters, 2009, Vol 583, Issue 20, p3323
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.09.034