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

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.

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

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: Netherlands
• Confidentiality degree: is not subject to a state or trade secret
• WWW: 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
• Tags: CF NMR, rivok
• Tags: International impact, Reviewed

Abstract

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

• LM2015043, research and development project: Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

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