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
Retrovirologyjournal_title
Retrovirologyauthors
Furnes C,Arnesen T,Askjaer P,Kjems J,Szilvay AMdoi
10.1186/1742-4690-2-39subject
Has Abstractpub_date
2005-06-10 00:00:00pages
39issn
1742-4690pii
1742-4690-2-39journal_volume
2pub_type
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