Linked Life Data

7520442

Source:http://linkedlifedata.com/resource/pubmed/id/7520442

Statements in which the resource exists.
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pubmed-article:7520442pubmed:abstractTextAn active p15 RNase H domain, consisting of amino acids 427-560 of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and a genetically engineered penta-histidine N-terminal affinity tag, was expressed in Escherichia coli and purified to apparent homogeneity by immobilized metal affinity chromatography. The purified p15 RNase H domain exhibited no substrate preference for [3H]poly(rG).poly(dC) compared to [3H]poly(rA).poly(dT), in contrast with the HIV-1 RT-associated RNase H, which showed a 30-fold preference for the former substrate. Unlike the HIV-1 RT-associated RNase H, when challenged with unlabeled substrate, the recombinant p15 RNase H domain was relatively nonprocessive in RNA degradative activity of the [3H]poly(rA).poly(dT) duplex. Kinetic studies using p15 RNase H showed substrate inhibition with an apparent K(i) value of 0.12 micron for the [3H]poly(rA).poly(dT) hybrid. Substrate inhibition was not observed for the HIV-1 RT-associated RNase H. The results show that the isolated p15 HIV-1 RNase H domain is functionally distinct from the recombinant HIV-1 RT-associated RNase H.lld:pubmed
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pubmed-article:7520442pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:7520442pubmed:articleTitleAn active recombinant p15 RNase H domain is functionally distinct from the RNase H domain associated with human immunodeficiency virus type 1 reverse transcriptase.lld:pubmed
pubmed-article:7520442pubmed:affiliationBiochemistry Research, Upjohn Laboratories, Kalamazoo, Michigan 49001.lld:pubmed
pubmed-article:7520442pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7520442pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:7520442pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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