PloS one, 2010-10, Vol.5 (10), p.e13202-e13202
2010
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Details
- Autor(en) / Beteiligte
- Titel
- Structural transformation of the tandem ubiquitin-interacting motifs in ataxin-3 and their cooperative interactions with ubiquitin chains
- Ist Teil von
- PloS one, 2010-10, Vol.5 (10), p.e13202-e13202
- Ort / Verlag
- United States: Public Library of Science
- Erscheinungsjahr
- 2010
- Quelle
- Electronic Journals Library
- Beschreibungen/Notizen
- The ubiquitin-interacting motif (UIM) is a short peptide with dual function of binding ubiquitin (Ub) and promoting ubiquitination. We elucidated the structures and dynamics of the tandem UIMs of ataxin-3 (AT3-UIM12) both in free and Ub-bound forms. The solution structure of free AT3-UIM12 consists of two α-helices and a flexible linker, whereas that of the Ub-bound form is much more compact with hydrophobic contacts between the two helices. NMR dynamics indicates that the flexible linker becomes rigid when AT3-UIM12 binds with Ub. Isothermal titration calorimetry and NMR titration demonstrate that AT3-UIM12 binds diUb with two distinct affinities, and the linker plays a critical role in association of the two helices in diUb binding. These results provide an implication that the tandem UIM12 interacts with Ub or diUb in a cooperative manner through an allosteric effect and dynamics change of the linker region, which might be related to its recognitions with various Ub chains and ubiquitinated substrates.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1932-6203eISSN: 1932-6203DOI: 10.1371/journal.pone.0013202Titel-ID: cdi_plos_journals_1292426924
- Format
- –
- Schlagworte
- Allosteric properties, Ataxin, Ataxin-3, Binding, Biochemistry, Biochemistry/Biomacromolecule-Ligand Interactions, Biochemistry/Protein Folding, Biophysics, Calorimetry, Chains, Deoxyribonucleic acid, DNA, DNA polymerase, E coli, Escherichia coli, Helices, Hydrophobicity, Laboratories, Models, Molecular, Molecular biology, Nerve Tissue Proteins - chemistry, Nerve Tissue Proteins - metabolism, NMR, Nuclear magnetic resonance, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins - chemistry, Nuclear Proteins - metabolism, Peptides, Protein Binding, Protein Conformation, Proteins, Repressor Proteins - chemistry, Repressor Proteins - metabolism, Substrates, Titration, Titration calorimetry, Transformation, Ubiquitin, Ubiquitin - metabolism, Ubiquitination