HIV-1 Rev oligomerization is not obligatory in the presence of an extra basic domain.

Abstract:

BACKGROUND:The HIV-1 Rev regulatory protein binds as an oligomeric complex to viral RNA mediating nuclear export of incompletely spliced and non-spliced viral mRNAs encoding the viral structural proteins. However, the biological significance of the obligatory complex formation of Rev upon the viral RNA is unclear. RESULTS:The activity of various fusion proteins based on the negative oligomerization-defect Rev mutant M4 was tested using Rev dependent reporter constructs. An artificial M4 mutant dimer and an M4 mutant containing an extra basic domain from the HTLV-I Rex protein exhibited nearly full activity when compared to wild type Rev. CONCLUSION:Rev dimerization appears to be required to expose free basic domains whilst the Rev oligomeric complex remains bound to viral RNA via other basic domains.

journal_name

Retrovirology

journal_title

Retrovirology

authors

Furnes C,Arnesen T,Askjaer P,Kjems J,Szilvay AM

doi

10.1186/1742-4690-2-39

subject

Has Abstract

pub_date

2005-06-10 00:00:00

pages

39

issn

1742-4690

pii

1742-4690-2-39

journal_volume

2

pub_type

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