{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:55:21Z","timestamp":1781106921671,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"3","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1992,2]]},"abstract":"<jats:p>Early events in the retroviral replication cycle include the conversion of viral genomic RNA into linear double-stranded DNA. This process is mediated by the reverse transcriptase (RT), a multifunctional enzyme that possesses RNA-dependent DNA polymerase, DNA-dependent DNA polymerase, and RNase H activities. In the course of studies of a recombinant RT of human immunodeficiency virus type 1 (HIV-1), we observed an additional, unexpected activity of the enzyme. The purified RT catalyzes a specific cleavage in HIV-1 RNA hybridized to tRNALys, the primer for HIV-1 reverse transcription. The cleavage at the primer binding site (PBS) of HIV RNA is dependent on the double-stranded structure of the HIV RNA-tRNALys complex. This RNase activity appears to be distinct from the RNase H activity of HIV-1 RT, as the substrate specificity and the products of the two activities are different. Moreover, Escherichia coli RNase H and avian myeloblastosis virus RT are unable to cleave the HIV RNA-tRNALys complex. We refer to this unusual activity as RNase D. Two lines of evidence indicate that the specific RNase D activity is an integral part of recombinant HIV RT. The specific RNase D activity comigrates with the other RT activities, DNA polymerase, and RNase H upon filtration on a Superose 6 gel column or chromatography on a phosphocellulose column. Moreover, three recombinant HIV-1 RT preparations expressed and purified in different laboratories by various procedures exhibit RNase D activity. Sequence analysis indicated that RNase D activity cleaves the substrate HIV-1 RNA-tRNALys at two distinct sites within the PBS sequence 5'-UGGCGCCCGA decreases ACAG decreases GGAC-3'. The sequence specificity of RNase D activity suggests that it might be involved in two stages during the reverse transcription process: displacement of the PBS to enable copying of tRNALys sequences into plus-strand DNA or to facilitate the second template switch, which was postulated to occur at the PBS sequence.<\/jats:p>","DOI":"10.1073\/pnas.89.3.927","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T08:15:23Z","timestamp":1149063323000},"page":"927-931","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":25,"title":["Double-stranded RNA-dependent RNase activity associated with human immunodeficiency virus type 1 reverse transcriptase."],"prefix":"10.1073","volume":"89","author":[{"given":"H","family":"Ben-Artzi","sequence":"first","affiliation":[{"name":"BioTechnology General Ltd., Kiryat Weizmann, Rehovot, Israel."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E","family":"Zeelon","sequence":"additional","affiliation":[{"name":"BioTechnology General Ltd., Kiryat Weizmann, Rehovot, Israel."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Gorecki","sequence":"additional","affiliation":[{"name":"BioTechnology General Ltd., Kiryat Weizmann, Rehovot, Israel."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Panet","sequence":"additional","affiliation":[{"name":"BioTechnology General Ltd., Kiryat Weizmann, Rehovot, Israel."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1992,2]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.89.3.927","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T13:35:30Z","timestamp":1649856930000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.89.3.927"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,2]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1992,2]]}},"alternative-id":["10.1073\/pnas.89.3.927"],"URL":"https:\/\/doi.org\/10.1073\/pnas.89.3.927","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,2]]},"assertion":[{"value":"1992-02-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}