共查询到20条相似文献,搜索用时 23 毫秒
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Shah FS Curr KA Hamburgh ME Parniak M Mitsuya H Arnez JG Prasad VR 《The Journal of biological chemistry》2000,275(35):27037-27044
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Deval J Alvarez K Selmi B Bermond M Boretto J Guerreiro C Mulard L Canard B 《The Journal of biological chemistry》2005,280(5):3838-3846
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Deval J Navarro JM Selmi B Courcambeck J Boretto J Halfon P Garrido-Urbani S Sire J Canard B 《The Journal of biological chemistry》2004,279(24):25489-25496
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Operario DJ Balakrishnan M Bambara RA Kim B 《The Journal of biological chemistry》2006,281(43):32113-32121
We have recently demonstrated that HIV-1 RT mutants characterized by low dNTP binding affinity display significantly reduced dNTP incorporation kinetics in comparison to wild-type RT. This defect is particularly emphasized at low dNTP concentrations where WT RT remains capable of efficient synthesis. Kinetic interference in DNA synthesis can induce RT pausing and slow down the synthesis rate. RT stalling and slow synthesis rate can enhance RNA template cleavage by RT-RNase H, facilitating transfer of the primer to a homologous template. We therefore hypothesized that reduced dNTP binding RT mutants can promote template switching during minus strand synthesis more efficiently than WT HIV-1 RT at low dNTP concentrations. To test this hypothesis, we employed two dNTP binding HIV-1 RT mutants, Q151N and V148I. Indeed, as the dNTP concentration was decreased, the template switching frequency progressively increased for both WT and mutant RTs. However, as predicted, the RT mutants promoted more transfers compared with WT RT. The WT and mutant RTs were similar in their intrinsic RNase H activity, supporting that the elevated template switching efficiency of the mutants was not the result of the mutations enhancing RNase H activity. Rather, kinetic interference leading to stalled DNA synthesis likely enhanced transfers. These results suggest that the RT-dNTP substrate interaction mechanistically influences strand transfer and recombination of HIV-1 RT. 相似文献
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YADD mutants of human immunodeficiency virus type 1 and Moloney murine leukemia virus reverse transcriptase are resistant to lamivudine triphosphate (3TCTP) in vitro.
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Paul L. Boyer Hong-Qiang Gao Patrick K. Clark Stefan G. Sarafianos Edward Arnold Stephen H. Hughes 《Journal of virology》2001,75(14):6321-6328
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B Kim J C Ayran S G Sagar E T Adman S M Fuller N H Tran J Horrigan 《The Journal of biological chemistry》1999,274(39):27666-27673