期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 428, 期 1, 页码 79-91出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2015.11.023
关键词
Tau protein; proline conformation; cis/trans isomerisation; exchange spectroscopy; nuclear magnetic resonance spectroscopy
资金
- Complix (Ghent, Belgium)
- Region Nord-Pas de Calais
- CNRS
- Pasteur Institute of Lille
- European Community (FEDER)
- French Research Ministry
- University of Sciences and Technologies of Lille I
- TGE RMN THC (France) [FR-3050]
- Laboratory of Excellence, Development of Innovative Strategies for a Transdisciplinary Approach to Alzheimer's disease
The conformational state of distinct prolines can determine the folding of a protein but equally other biological processes when coupled to a conformation-sensitive secondary reaction. For the neuronal tau protein, the importance of proline conformation is underscored by its interaction with different prolyl cis/trans isomerases. The proline conformation would gain even further importance after phosphorylation of the preceding residue by various proline-directed kinases. A number of molecular diseases including Alzheimer's disease and traumatic brain injury were thereby recently qualified as cistauosis, as they would imply a cis conformation for the pThr231-Pro232 prolyl bond. We here investigate by NMR spectroscopy the conformation of all prolines in a functional Tau fragment, Tau[208-324]. Although we can detect and identify some minor conformers in the cis form, we show that all prolines are for over 90% in the trans conformation. Phosphorylation by CDK2/CycA3, which notably leads to complete modification of the Thr231 residue, does not change this conclusion. Our data hence disagree with the notion that specific prolyl bonds in tau would adopt preferentially the cis conformation. (C) 2015 Elsevier Ltd. All rights reserved.
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