Evidence that less-than-full-length pol gene products are functional in hepadnavirus DNA synthesis.

Abstract:

:Duck hepatitis B virus mutants containing frameshift or stop codon mutations in a portion of the viral pol gene separating the terminal protein and reverse transcriptase domains had a leaky phenotype and, depending on the location and type of mutation, synthesized up to 10% as much viral DNA as did the wild type. This region of the pol gene had previously been reported to be refractory to missense mutations; in fact, the leakiness of most of our mutants appeared attributable to translational suppression, which would also be expected to introduce amino acid changes. However, at least one mutant (pH1093 + 2), which was ca. 10% as active as the wild type, appeared to use a novel pathway to express the viral pol gene. Our analyses indicated that pH1093 + 2 synthesized the viral reverse transcriptase as a fusion protein with the amino-terminal portion of the pre-S envelope protein. Thus, in this case, the products of the terminal-protein and reverse transcriptase domains of the pol gene would function as separate protein species, though perhaps noncovalently joined in a dimeric structure during assembly of DNA replication complexes. Evidence was also obtained that was consistent with the idea that the wild-type pol gene may, at least in certain instances, be expressed as functional, subgenic polypeptides.

journal_name

J Virol

journal_title

Journal of virology

authors

Wu TT,Condreay LD,Coates L,Aldrich C,Mason W

doi

10.1128/JVI.65.5.2155-2163.1991

subject

Has Abstract

pub_date

1991-05-01 00:00:00

pages

2155-63

issue

5

eissn

0022-538X

issn

1098-5514

journal_volume

65

pub_type

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