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.

Základní údaje

Originální název

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

Autoři

LOUŠA, Petr (203 Česká republika, domácí), Hana NEDOZRÁLOVÁ (203 Česká republika, domácí), Erik ŽUPA (703 Slovensko, domácí), Jiří NOVÁČEK (203 Česká republika, domácí) a Jozef HRITZ (703 Slovensko, garant, domácí)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 1.870

Kód RIV

RIV/00216224:14740/17:00094769

Organizační jednotka

Středoevropský technologický institut

DOI

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

UT WoS

000398010000004

Klíčová slova anglicky

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

Štítky

CF NMR, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 1. 6. 2017 11:35, Mgr. Petr Louša, Ph.D.

Anotace

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.

Návaznosti

GF15-34684L, projekt VaV

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

Investor: Grantová agentura ČR, Efektivní výpočty volných energií a konfiguračního vzorkování protein-proteinových interakcí, Partnerská agentura (Rakousko)

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

Citovat

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

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