Bacterial expression of human respiratory syncytial viral phosphoprotein P and identification of Ser237 as the site of phosphorylation by cellular casein kinase II.
Virology
; 205(1): 93-103, 1994 Nov 15.
Article
en En
| MEDLINE
| ID: mdl-7975241
ABSTRACT
The phosphoprotein P gene of human respiratory syncytial virus has been cloned and the protein expressed in Escherichia coli. The expressed protein was soluble, unphosphorylated, and constituted approximately 10% of the total bacterial protein. Electrophoretic and antigenic analyses demonstrated the identity of the recombinant protein with viral P protein and P protein synthesized in reticulocyte lysates. Purified recombinant P protein was efficiently phosphorylated in vitro by purified native as well as recombinant casein kinase II (CKII) or by the CKII activity in uninfected cell extracts. Through deletions and site-directed mutagenesis, the site of CKII phosphorylation was mapped to a single serine residue (Ser237) near the C-terminal end of the P protein.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Virus Sincitiales Respiratorios
/
Serina
/
Proteínas Virales
/
Proteína HN
/
Proteínas Serina-Treonina Quinasas
/
Escherichia coli
Tipo de estudio:
Diagnostic_studies
Límite:
Humans
Idioma:
En
Revista:
Virology
Año:
1994
Tipo del documento:
Article