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  4. Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase
 
research article

Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase

Sánchez, Ricardo
•
Pantoja-Uceda, David
•
Prieto, Jesús
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2010
Journal of Biological Chemistry

Gadd45alpha is a nuclear protein encoded by a DNA damage-inducible gene. Through its interactions with other proteins, Gadd45alpha participates in the regulation of DNA repair, cell cycle, cell proliferation, and apoptosis. The NMR structure of human Gadd45alpha has been determined and shows an alpha/beta fold with two long disordered and flexible regions at the N terminus and one of the loops. Human Gadd45alpha is predominantly monomeric in solution but exists in equilibrium with dimers and other oligomers whose population increases with protein concentration. NMR analysis shows that Aurora A interacts through its N-terminal domain with a region of human Gadd45alpha encompassing the site of dimerization, suggesting that the oligomerization of Gadd45alpha could be a regulatory mechanism to modulate its interactions with Aurora A, and possibly with other proteins too. However, Gadd45alpha appears to interact only weakly with PCNA through its flexible loop, in contrast with previous and contradictory reports.

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Type
research article
DOI
10.1074/jbc.M109.069344
Author(s)
Sánchez, Ricardo
Pantoja-Uceda, David
Prieto, Jesús
Diercks, Tammo
Marcaida, María J
Montoya, Guillermo
Campos-Olivas, Ramón
Blanco, Francisco J
Date Issued

2010

Publisher

American Society for Biochemistry and Molecular Biology

Published in
Journal of Biological Chemistry
Volume

285

Issue

29

Start page

22196

End page

201

Editorial or Peer reviewed

NON-REVIEWED

Written at

EPFL

EPFL units
IBI-SV  
Available on Infoscience
November 17, 2016
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/131166
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