Mutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity.
J Virol
; 64(2): 613-20, 1990 Feb.
Article
em En
| MEDLINE
| ID: mdl-2153228
ABSTRACT
To correlate the hepatitis B virus P gene with the enzymatic activities predicted to participate in hepadnavirus reverse transcription, a series of P gene mutants containing missense mutations, in-phase insertions, and in-phase deletions was constructed by site-directed mutagenesis. These mutants were tested in the context of otherwise intact hepatitis B virus genomes for the ability to produce core particles containing the virus-associated polymerase activity. The results obtained suggest that the P protein consists of three functional domains and a nonessential spacer arranged in the following order terminal protein, spacer, reverse transcriptase/DNA polymerase, and RNase H. The first two domains are separated by a spacer region which could be deleted to a large extent without significant loss of endogenous polymerase activity. In cotransfection experiments, all P gene mutants could be complemented in trans by constructs expressing the wild-type gene product but not by a second P gene mutant. This indicates that the multifunctional P gene is expressed as a single translational unit and independent of the core gene and furthermore that the gene product is freely diffusible and not processed before core assembly.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Estruturais Virais
/
Vírus da Hepatite B
/
Endorribonucleases
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Genes Virais
/
Mutação
Limite:
Humans
Idioma:
En
Revista:
J Virol
Ano de publicação:
1990
Tipo de documento:
Article