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

J 2017

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

LOUŠA, Petr, Hana NEDOZRÁLOVÁ, Erik ŽUPA, Jiří NOVÁČEK, Jozef HRITZ et. al.

Basic information

Original name

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

Authors

LOUŠA, Petr (203 Czech Republic, belonging to the institution), Hana NEDOZRÁLOVÁ (203 Czech Republic, belonging to the institution), Erik ŽUPA (703 Slovakia, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution) and Jozef HRITZ (703 Slovakia, guarantor, belonging to the institution)

Edition

Biophysical Chemistry, AMSTERDAM, Elsevier, 2017, 0301-4622

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 1.870

RIV identification code

RIV/00216224:14740/17:00094769

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1016/j.bpc.2017.01.003

UT WoS

000398010000004

Keywords in English

Human tyrosine hydroxylase; IDP; NMR; Phosphorylation; Kinetics; Time-resolved NMR; Non-uniform sampling; SSP

Abstract

V originále

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.

Links

GF15-34684L, research and development project

Name: Efektivní výpočty volných energií a konfiguračního vzorkování protein-‐proteinových interakcí

Investor: Czech Science Foundation, Partner Agency (Austria)

LM2015043, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

LOUŠA, Petr, Hana NEDOZRÁLOVÁ, Erik ŽUPA, Jiří NOVÁČEK and Jozef HRITZ. Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR. Biophysical Chemistry. AMSTERDAM: Elsevier, 2017, vol. 223, April, p. 25-29. ISSN 0301-4622. Available from: https://dx.doi.org/10.1016/j.bpc.2017.01.003.

@article{1381948,
   author = {Louša, Petr and Nedozrálová, Hana and Župa, Erik and Nováček, Jiří and Hritz, Jozef},
   article_location = {AMSTERDAM},
   article_number = {April},
   doi = {http://dx.doi.org/10.1016/j.bpc.2017.01.003},
   keywords = {Human tyrosine hydroxylase; IDP; NMR; Phosphorylation; Kinetics; Time-resolved NMR; Non-uniform sampling; SSP},
   language = {eng},
   issn = {0301-4622},
   journal = {Biophysical Chemistry},
   title = {Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR},
   url = {http://www.sciencedirect.com/science/article/pii/S0301462216304999},
   volume = {223},
   year = {2017}
}

TY  - JOUR
ID  - 1381948
AU  - Louša, Petr - Nedozrálová, Hana - Župa, Erik - Nováček, Jiří - Hritz, Jozef
PY  - 2017
TI  - Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR
JF  - Biophysical Chemistry
VL  - 223
IS  - April
SP  - 25-29
EP  - 25-29
PB  - Elsevier
SN  - 03014622
KW  - Human tyrosine hydroxylase
KW  - IDP
KW  - NMR
KW  - Phosphorylation
KW  - Kinetics
KW  - Time-resolved NMR
KW  - Non-uniform sampling
KW  - SSP
UR  - http://www.sciencedirect.com/science/article/pii/S0301462216304999
L2  - http://www.sciencedirect.com/science/article/pii/S0301462216304999
N2  - 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.
ER  -

LOUŠA, Petr, Hana NEDOZRÁLOVÁ, Erik ŽUPA, Jiří NOVÁČEK and Jozef HRITZ. Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR. \textit{Biophysical Chemistry}. AMSTERDAM: Elsevier, 2017, vol.~223, April, p.~25-29. ISSN~0301-4622. Available from: https://dx.doi.org/10.1016/j.bpc.2017.01.003.

Detailed Information on Publication Record