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Default NMR analysis of the acetylation pattern of the neuronal Tau protein.

NMR analysis of the acetylation pattern of the neuronal Tau protein.

NMR analysis of the acetylation pattern of the neuronal Tau protein.

Biochemistry. 2014 Apr 7;

Authors: Kamah A, Huvent I, Cantrelle FX, Qi H, Lippens G, Landrieu I, Smet-Nocca C

Abstract
Lysine acetylation of the neuronal Tau protein was described as a novel mechanism of posttranslational regulation of Tau functions with important outcomes in microtubule binding and aggregation processes related to Alzheimer's disease. Here, we unravel at a per-residue resolution the acetylation pattern of full-length Tau by the Creb-binding protein (CBP) acetyltransferase using high-resolution NMR spectroscopy. Our study gives a quantitative overview of CBP-mediated acetylation and examines the catalytic proficiency since non-enzymatic reaction with acetyl-coenzyme A occurs in vitro. Furthermore, we have investigated with this characterized acetylated Tau the effect of acetylation on Tau fibrillization in a heparin-induced aggregation assay and on heparin binding.


PMID: 24708343 [PubMed - as supplied by publisher]



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