The N-terminal amino acid sequence is essential for foot-and-mouth disease virus replicase activity
Rev. bras. pesqui. méd. biol
; Braz. j. med. biol. res;25(7): 659-66, 1992. ilus, tab
Article
en En
| LILACS
| ID: lil-113555
Biblioteca responsable:
BR26.1
ABSTRACT
Foot-and-mouth disease virus replicase was expressed by fusing its cDNA to the OmpA signal peptide coding sequence present in the pIN-III ompA series vectors. Two constructions were developed to express either a full-lenghtt or truncated enzyme lacking the 20 aminoacids at the N-terminal en. Bacterial extr5acts expressing the recombinant proteins were submitted to SDS-PAGE and the presence of the replicase was revealed by immunoblotting. The truncated form exhibited a higher mobility and the relative positions of the proteins show that the signal peptide was removed. The biological activity of these two molecules was tested using a poly(A)-dep[endent oligo(U)-primed poly(U)-polymer4ase assay. The full-lenght replicase is active. The aminoterminal truncated wnzyme had 0.02% activity o9f the intact5 one. This result indicates the importaqnce of the twenty N-terminal amino acids for the activity of FMDV RNA dependent RNMA polymerase
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Colección:
01-internacional
Base de datos:
LILACS
Asunto principal:
Péptidos
/
Replicación Viral
/
ARN Polimerasa Dependiente del ARN
/
Secuencia de Aminoácidos
/
Fiebre Aftosa
Idioma:
En
Revista:
Braz. j. med. biol. res
/
Rev. bras. pesqui. méd. biol
Asunto de la revista:
BIOLOGIA
/
MEDICINA
Año:
1992
Tipo del documento:
Article
Pais de publicación:
Brasil