Targeted mutagenesis of the P22 portal protein reveals the mechanism of signal transmission during DNA packaging.
Virology
; 505: 127-138, 2017 05.
Article
en En
| MEDLINE
| ID: mdl-28242514
ABSTRACT
The portal vertex in dsDNA bacteriophage serves as the site for genome encapsidation and release. In several of these viruses, efficient termination of DNA packaging has been shown to be dependent on the density of packaged DNA. The portal protein has been implicated as being part of the sensor that regulates packaging termination through DNA-dependent conformational changes during packaging. The mechanism by which DNA induces these conformational changes remains unknown. In this study, we explore how point mutants in the portal core can result in changes in genome packaging density in P22. Mutations in the portal core that subtly alter the structure or dynamics of the protein result in an increase in the amount of DNA packaged. The magnitude of the change is amino acid and location specific. Our findings suggest a mechanism wherein compression of the portal core is an essential aspect of signal transmission during packaging.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Salmonella
/
ADN Viral
/
Bacteriófago P22
/
Ensamble de Virus
/
Proteínas de la Cápside
/
Empaquetamiento del ADN
Idioma:
En
Revista:
Virology
Año:
2017
Tipo del documento:
Article
País de afiliación:
Estados Unidos