Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus.
Virology
; 337(1): 162-74, 2005 Jun 20.
Article
em En
| MEDLINE
| ID: mdl-15914229
ABSTRACT
The major inducible 70-kDa heat shock protein (hsp72) binds measles virus (MV) nucleocapsids and increases MV gene expression. The cytoplasmic tail of the MV N protein (N(TAIL)) contains three hydrophobic domains (Box-1-3) that are potential targets of hsp72 interaction. Low affinity binding to Box-3 is correlated to hsp72-dependent stimulation of MV minireplicon reporter gene expression whereas interactions between hsp72 and Box-1 and/or -2 have not been documented. The present work showed that virus deficient in Box-3/hsp72 interaction retains the ability to form nucleocapsid/hsp72 complexes, identifying Box-2 but not Box-1 as a mediator of high affinity hsp72 binding. Box-2 is the binding site for the viral P protein X domain (XD), where P tethers the viral polymerase to nucleocapsid in support of transcription and genome replication, and competitive inhibition of XD binding to N(TAIL) by hsp72 was shown. Recognition of a common binding site by P and hsp72 represents a potential mechanism for host cell modulation of viral gene expression.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas do Nucleocapsídeo
/
Proteínas de Choque Térmico
/
Vírus do Sarampo
Limite:
Humans
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article