Journal of Biological Chemistry
ArticleVirion-associated, host-derived DHX9/RNA helicase A enhances the processivity of HIV-1 reverse transcriptase on genomic RNADHX9/RHA enhances RT's processivity
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This work was supported by National Institutes of Health Grant R01AI150460 (reassigned from R01GM119932; to X. H. and K.-B.-L.) and R01CA108882 (to K. B.-L). The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
This article contains Table S1.
- 1
Present address: Intrexon Corporation, Gaithersburg, MD 20876.
- 2
Present address: College of Sciences, Lucian Blaga University, Sibiu, Romania, 550012.
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The abbreviations used are:
- HIV-1
human immunodeficiency virus, type 1
- RHA
RNA helicase A
- RNP
reverse-transcription ribonucleoprotein
- RT
reverse transcriptase
- CA
capsid
- nt
nucleotide(s)
- PBS
primer-binding site
- NC
nucleocapsid
- dsRBD
dsRNA-binding domain
- qPCR
quantitative PCR
- NT siRNA
nontargeting siRNA
- P/T
primer–template
- ddATP
dideoxyATP
- FTSC
fluorescein-5-thiosemicarbazide.