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

Warning

This publication doesn't include Faculty of Education. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

LOUŠA Petr NEDOZRÁLOVÁ Hana ŽUPA Erik NOVÁČEK Jiří HRITZ Jozef

Year of publication 2017
Type Article in Periodical
Magazine / Source Biophysical Chemistry
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.sciencedirect.com/science/article/pii/S0301462216304999
Doi http://dx.doi.org/10.1016/j.bpc.2017.01.003
Field Biochemistry
Keywords Human tyrosine hydroxylase; IDP; NMR; Phosphorylation; Kinetics; Time-resolved NMR; Non-uniform sampling; SSP
Description 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.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.