Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.

The stress protein Nupr1 is a highly basic, multifunctional, intrinsically disordered protein (IDP). MSL1 is a histone acetyl transferase-associated protein, known to intervene in the dosage compensation complex (DCC). In this work, we show that both Nupr1 and MSL1 proteins were recruited and formed...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	David Aguado-Llera, Tewfik Hamidi, Rosa Doménech, David Pantoja-Uceda, Meritxell Gironella, Jorge Santoro, Adrián Velázquez-Campoy, José L Neira, Juan L Iovanna
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5d92fd0d15044e9892b0fd93e7dfb61c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:5d92fd0d15044e9892b0fd93e7dfb61c
record_format	dspace
spelling	oai:doaj.org-article:5d92fd0d15044e9892b0fd93e7dfb61c2021-11-18T08:48:55ZDeciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.1932-620310.1371/journal.pone.0078101https://doaj.org/article/5d92fd0d15044e9892b0fd93e7dfb61c2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24205110/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The stress protein Nupr1 is a highly basic, multifunctional, intrinsically disordered protein (IDP). MSL1 is a histone acetyl transferase-associated protein, known to intervene in the dosage compensation complex (DCC). In this work, we show that both Nupr1 and MSL1 proteins were recruited and formed a complex into the nucleus in response to DNA-damage, which was essential for cell survival in reply to cisplatin damage. We studied the interaction of Nupr1 and MSL1, and their binding affinities to DNA by spectroscopic and biophysical methods. The MSL1 bound to Nupr1, with a moderate affinity (2.8 µM) in an entropically-driven process. MSL1 did not bind to non-damaged DNA, but it bound to chemically-damaged-DNA with a moderate affinity (1.2 µM) also in an entropically-driven process. The Nupr1 protein bound to chemically-damaged-DNA with a slightly larger affinity (0.4 µM), but in an enthalpically-driven process. Nupr1 showed different interacting regions in the formed complexes with Nupr1 or DNA; however, they were always disordered ("fuzzy"), as shown by NMR. These results underline a stochastic description of the functionality of the Nupr1 and its other interacting partners.David Aguado-LleraTewfik HamidiRosa DoménechDavid Pantoja-UcedaMeritxell GironellaJorge SantoroAdrián Velázquez-CampoyJosé L NeiraJuan L IovannaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e78101 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q David Aguado-Llera Tewfik Hamidi Rosa Doménech David Pantoja-Uceda Meritxell Gironella Jorge Santoro Adrián Velázquez-Campoy José L Neira Juan L Iovanna Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.
description	The stress protein Nupr1 is a highly basic, multifunctional, intrinsically disordered protein (IDP). MSL1 is a histone acetyl transferase-associated protein, known to intervene in the dosage compensation complex (DCC). In this work, we show that both Nupr1 and MSL1 proteins were recruited and formed a complex into the nucleus in response to DNA-damage, which was essential for cell survival in reply to cisplatin damage. We studied the interaction of Nupr1 and MSL1, and their binding affinities to DNA by spectroscopic and biophysical methods. The MSL1 bound to Nupr1, with a moderate affinity (2.8 µM) in an entropically-driven process. MSL1 did not bind to non-damaged DNA, but it bound to chemically-damaged-DNA with a moderate affinity (1.2 µM) also in an entropically-driven process. The Nupr1 protein bound to chemically-damaged-DNA with a slightly larger affinity (0.4 µM), but in an enthalpically-driven process. Nupr1 showed different interacting regions in the formed complexes with Nupr1 or DNA; however, they were always disordered ("fuzzy"), as shown by NMR. These results underline a stochastic description of the functionality of the Nupr1 and its other interacting partners.
format	article
author	David Aguado-Llera Tewfik Hamidi Rosa Doménech David Pantoja-Uceda Meritxell Gironella Jorge Santoro Adrián Velázquez-Campoy José L Neira Juan L Iovanna
author_facet	David Aguado-Llera Tewfik Hamidi Rosa Doménech David Pantoja-Uceda Meritxell Gironella Jorge Santoro Adrián Velázquez-Campoy José L Neira Juan L Iovanna
author_sort	David Aguado-Llera
title	Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.
title_short	Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.
title_full	Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.
title_fullStr	Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.
title_full_unstemmed	Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.
title_sort	deciphering the binding between nupr1 and msl1 and their dna-repairing activity.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/5d92fd0d15044e9892b0fd93e7dfb61c
work_keys_str_mv	AT davidaguadollera decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT tewfikhamidi decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT rosadomenech decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT davidpantojauceda decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT meritxellgironella decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT jorgesantoro decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT adrianvelazquezcampoy decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT joselneira decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity AT juanliovanna decipheringthebindingbetweennupr1andmsl1andtheirdnarepairingactivity
_version_	1718421264428695552

Deciphering the binding between Nupr1 and MSL1 and their DNA-repairing activity.

Ejemplares similares