Dissection of Binding between a Phosphorylated Tyrosine
Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated
by NMR

J 2014

Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR

HRITZ, Jozef, In-Ja L. BYEON, Troyi KRZYSIAK, Aurora MARTINEZ, Vladimír SKLENÁŘ et. al.

Basic information

Original name

Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR

Authors

HRITZ, Jozef (703 Slovakia, guarantor, belonging to the institution), In-Ja L. BYEON (840 United States of America), Troyi KRZYSIAK (840 United States of America), Aurora MARTINEZ (578 Norway), Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution) and Angela M. GRONENBORN (840 United States of America)

Edition

Biophysical Journal, New York, USA, Cell Press, 2014, 0006-3495

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10610 Biophysics

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.972

RIV identification code

RIV/00216224:14740/14:00077266

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1016/j.bpj.2014.08.039

UT WoS

000344232500020

Keywords in English

STRUCTURAL BASIS; PROTEINS; DOMAIN; SITES; GENE

Abstract

V originále

Human tyrosine hydroxylase activity is regulated by phosphorylation of its N-terminus and by an interaction with the modulator 14-3-3 proteins. We investigated the binding of singly or doubly phosphorylated and thiophosphorylated peptides, comprising the first 50 amino acids of human tyrosine hydroxylase, isoform 1 (hTH1), that contain the critical interaction domain, to 14-3-3zéta, by 31P NMR. Single phosphorylation at S19 generates a high affinity 14-3-3zéta binding epitope, whereas singly S40-phosphorylated peptide interacts with 14-3-3zéta one order-of-magnitude weaker than the S19-phosphorylated peptide. Analysis of the binding data revealed that the 14-3-3zéta dimer and the S19- and S40-doubly phosphorylated peptide interact in multiple ways, with three major complexes formed: 1), a single peptide bound to a 14-3-3zéta dimer via the S19 phosphate with the S40 phosphate occupying the other binding site; 2), a single peptide bound to a 14-3-3zéta dimer via the S19 phosphorous with the S40 free in solution; or 3), a 14-3-3zéta dimer with two peptides bound via the S19 phosphorous to each binding site. Our system and data provide information as to the possible mechanisms by which 14-3-3 can engage binding partners that possess two phosphorylation sites on flexible tails. Whether these will be realized in any particular interacting pair will naturally depend on the details of each system.

Citovat

HRITZ, Jozef, In-Ja L. BYEON, Troyi KRZYSIAK, Aurora MARTINEZ, Vladimír SKLENÁŘ and Angela M. GRONENBORN. Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR. Biophysical Journal. New York, USA: Cell Press, 2014, vol. 107, No 9, p. 2185-2194. ISSN 0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2014.08.039.

@article{1205665,
   author = {Hritz, Jozef and Byeon, InandJa L. and Krzysiak, Troyi and Martinez, Aurora and Sklenář, Vladimír and Gronenborn, Angela M.},
   article_location = {New York, USA},
   article_number = {9},
   doi = {http://dx.doi.org/10.1016/j.bpj.2014.08.039},
   keywords = {STRUCTURAL BASIS; PROTEINS; DOMAIN; SITES; GENE},
   language = {eng},
   issn = {0006-3495},
   journal = {Biophysical Journal},
   title = {Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR},
   url = {http://www.sciencedirect.com/science/article/pii/S0006349514010121},
   volume = {107},
   year = {2014}
}

TY  - JOUR
ID  - 1205665
AU  - Hritz, Jozef - Byeon, In-Ja L. - Krzysiak, Troyi - Martinez, Aurora - Sklenář, Vladimír - Gronenborn, Angela M.
PY  - 2014
TI  - Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR
JF  - Biophysical Journal
VL  - 107
IS  - 9
SP  - 2185-2194
EP  - 2185-2194
PB  - Cell Press
SN  - 00063495
KW  - STRUCTURAL BASIS
KW  - PROTEINS
KW  - DOMAIN
KW  - SITES
KW  - GENE
UR  - http://www.sciencedirect.com/science/article/pii/S0006349514010121
L2  - http://www.sciencedirect.com/science/article/pii/S0006349514010121
N2  - Human tyrosine hydroxylase activity is regulated by phosphorylation of its N-terminus and by an interaction with the modulator 14-3-3 proteins. We investigated the binding of singly or doubly phosphorylated and thiophosphorylated peptides, comprising the first 50 amino acids of human tyrosine hydroxylase, isoform 1 (hTH1), that contain the critical interaction domain, to 14-3-3zéta, by 31P NMR. Single phosphorylation at S19 generates a high affinity 14-3-3zéta binding epitope, whereas singly S40-phosphorylated peptide interacts with 14-3-3zéta one order-of-magnitude weaker than the S19-phosphorylated peptide. Analysis of the binding data revealed that the 14-3-3zéta dimer and the S19- and S40-doubly phosphorylated peptide interact in multiple ways, with three major complexes formed: 1), a single peptide bound to a 14-3-3zéta dimer via the S19 phosphate with the S40 phosphate occupying the other binding site; 2), a single peptide bound to a 14-3-3zéta dimer via the S19 phosphorous with the S40 free in solution; or 3), a 14-3-3zéta dimer with two peptides bound via the S19 phosphorous to each binding site. Our system and data provide information as to the possible mechanisms by which 14-3-3 can engage binding partners that possess two phosphorylation sites on flexible tails. Whether these will be realized in any particular interacting pair will naturally depend on the details of each system.
ER  -

HRITZ, Jozef, In-Ja L. BYEON, Troyi KRZYSIAK, Aurora MARTINEZ, Vladimír SKLENÁŘ and Angela M. GRONENBORN. Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR. \textit{Biophysical Journal}. New York, USA: Cell Press, 2014, vol.~107, No~9, p.~2185-2194. ISSN~0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2014.08.039.

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