Linker insertion mutagenesis of the human immunodeficiency virus reverse transcriptase expressed in bacteria: definition of the minimal polymerase domain.

AUTOR(ES)

Prasad, V R

RESUMO

A plasmid construct expressing the p66 version of the human immunodeficiency virus reverse transcriptase as a bacterial fusion protein was subjected to in vitro mutagenesis, and the resulting variant proteins were assayed to define the locations of the two major enzymatic activities. The DNA polymerase activity was localized to the N-terminal portion of the protein; mutations altering or eliminating the C-terminal portion had little or no effect on that activity. The results suggest that, in contrast with previous reports, the p51 subunit found in virions should exhibit DNA polymerase activity. Mutations in many parts of the protein eliminated RNase H activity, suggesting that several areas are needed for proper folding and generation of that activity.

Documentos Relacionados

• Domain structure of the human immunodeficiency virus reverse transcriptase.
• Mutational definition of the human immunodeficiency virus type 1 Rev activation domain.
• The human LINE-1 reverse transcriptase:effect of deletions outside the common reverse transcriptase domain.
• Cassette mutagenesis of the reverse transcriptase of human immunodeficiency virus type 1.
• Effect of linker insertion mutations in the human immunodeficiency virus type 1 gag gene on activation of viral protease expressed in bacteria.