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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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Proline Conformation in a Functional Tau Fragment.

Puneet Ahuja¹, François-Xavier Cantrelle¹, Isabelle Huvent¹

¹UMR8576 CNRS Lille University, 59658 Villeneuve d'Ascq, France.

Journal of Molecular Biology

|December 15, 2015

Summary

This summary is machine-generated.

Proline conformation in tau protein is crucial for its function and disease relevance. This study found that tau prolines are predominantly in the trans conformation, even after phosphorylation, challenging the "cistauosis" hypothesis in diseases like Alzheimer's.

Keywords:

Tau protein cis/trans isomerisation exchange spectroscopy nuclear magnetic resonance spectroscopy proline conformation

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Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Proline conformation influences protein folding and biological processes.
Proline's role in neuronal tau protein is significant, involving interactions with isomerases and kinases.
Diseases like Alzheimer's are linked to a specific cis proline conformation in tau (pThr231-Pro232), termed 'cistauosis'.

Purpose of the Study:

To investigate the conformational states of all prolines within a functional tau fragment (Tau[208-324]).
To determine the impact of phosphorylation at Thr231 on proline conformation.
To evaluate the validity of the 'cistauosis' hypothesis.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy was employed to analyze proline conformations.
A functional tau fragment, Tau[208-324], was used for the investigation.
Proline-directed phosphorylation was induced using CDK2/CycA3.

Main Results:

All prolines in the tau fragment were found to be predominantly in the trans conformation (>90%).
Minor cis conformers were detected but were not the dominant state.
Phosphorylation of Thr231 by CDK2/CycA3 did not alter the overall trans preference of the prolyl bonds.

Conclusions:

The study's findings contradict the hypothesis that specific tau prolyl bonds preferentially adopt a cis conformation.
The 'cistauosis' model, linking cis proline conformation to neurodegenerative diseases, requires re-evaluation based on these results.
Tau prolines largely maintain a trans conformation, irrespective of phosphorylation at Thr231.