Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR

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Publikace nespadá pod Filozofickou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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LOUŠA Petr NEDOZRÁLOVÁ Hana ŽUPA Erik NOVÁČEK Jiří HRITZ Jozef

Rok publikování 2017
Druh Článek v odborném periodiku
Časopis / Zdroj Biophysical Chemistry
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://www.sciencedirect.com/science/article/pii/S0301462216304999
Doi http://dx.doi.org/10.1016/j.bpc.2017.01.003
Obor Biochemie
Klíčová slova Human tyrosine hydroxylase; IDP; NMR; Phosphorylation; Kinetics; Time-resolved NMR; Non-uniform sampling; SSP
Popis Human tyrosine hydroxylase 1 (hTH1) activity is regulated by phosphorylation of its regulatory domain (RD-hTH1) and by an interaction with the 14-3-3 protein. The RD-hTH1 is composed of a structured region (66169) preceded by an intrinsically disordered protein region (IDP, hTH1_65) containing two phosphorylation sites (S19 and S40) which are highly relevant for its increase in activity. The NMR signals of the IDP region in the non-phosphorylated, singly phosphorylated (pS40) and doubly phosphorylated states (pS19_pS40) were assigned by non-uniformly sampled spectra with increased dimensionality (5D). The structural changes induced by phosphorylation were analyzed by means of secondary structure propensities. The phosphorylation kinetics of the S40 and S19 by kinases PKA and PRAK respectively were monitored by non-uniformly sampled time-resolved NMR spectroscopy followed by their quantitative analysis. (C) 2017 Elsevier B.V. All rights reserved.
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