HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation.

Détails

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Etat: Serval
Version: Final published version
ID Serval
serval:BIB_4B814222B1E9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Park J., Lammers F., Herr W., Song J.J.
ISSN
1091-6490 (Electronic)
ISSN-L
0027-8424
Statut éditorial
Publié
Date de publication
2012
Volume
109
Numéro
43
Pages
17430-17435
Langue
anglais
Résumé
Host-cell factor 1 (HCF-1) is an unusual transcriptional regulator that undergoes a process of proteolytic maturation to generate N- (HCF-1(N)) and C- (HCF-1(C)) terminal subunits noncovalently associated via self-association sequence elements. Here, we present the crystal structure of the self-association sequence 1 (SAS1) including the adjacent C-terminal HCF-1 nuclear localization signal (NLS). SAS1 elements from each of the HCF-1(N) and HCF-1(C) subunits form an interdigitated fibronectin type 3 (Fn3) tandem repeat structure. We show that the C-terminal NLS recruited by the interdigitated SAS1 structure is required for effective formation of a transcriptional regulatory complex: the herpes simplex virus VP16-induced complex. Thus, HCF-1(N)-HCF-1(C) association via an integrated Fn3 structure permits an NLS to facilitate formation of a transcriptional regulatory complex.
Mots-clé
Amino Acid Sequence, Crystallography, X-Ray, Gene Expression Regulation, Host Cell Factor C1/chemistry, Host Cell Factor C1/physiology, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Localization Signals, Tandem Repeat Sequences, Transcription, Genetic
Pubmed
Web of science
Open Access
Oui
Création de la notice
06/12/2012 19:52
Dernière modification de la notice
08/05/2019 18:14
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