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Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
- Source :
-
Virology . Jun2005, Vol. 337 Issue 1, p162-174. 13p. - Publication Year :
- 2005
-
Abstract
- 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 (NTAIL) 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 NTAIL 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. [Copyright &y& Elsevier]
- Subjects :
- *GENE expression
*HEAT shock proteins
*VIRUS diseases
*PARAMYXOVIRUSES
Subjects
Details
- Language :
- English
- ISSN :
- 00426822
- Volume :
- 337
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Virology
- Publication Type :
- Academic Journal
- Accession number :
- 17855654
- Full Text :
- https://doi.org/10.1016/j.virol.2005.03.035