Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: The connection domain in reverse transcriptase facilitates the in vivo annealing of tRNALys3 to HIV-1 genomic RNA | Retrovirology BioMed Central Research Open Access The connection domain in reverse transcriptase facilitates the in vivo annealing of tRNALys3 to HIV-I genomic RNA Shan Cen1 2 Meijuan Niu2 and Lawrence Kleiman 1 2 3 Address 1Lady Davis Institute for Medical Research and McGill AIDS Centre Jewish General Hospital Montreal Quebec Canada H3T 1E2 2Department of Medicine McGill University Montreal Quebec Canada H3T 1E2 and 3Department of Microbiology and Immunology McGill University Montreal Quebec Canada H3T 1E2 Email Shan Cen - MeijuanNiu - meijuann@ Lawrence Kleiman - Corresponding author Published 19 October 2004 Received 23 August 2004 Accepted 19 October 2004 Retrovirology 2004 1 33 doi l742-4690-l-33 This article is available from http content l l 33 2004 Cen et al licensee BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract The primer tRNA for reverse transcription in HIV-l tRNALys3 is selectively packaged into the virus during its assembly and annealed to the viral genomic RNA. The ribonucleoprotein complex that is involved in the packaging and annealing of tRNALys into HIV-l consists of Gag GagPol tRNALys lysyl-tRNA synthetase LysRS and viral genomic RNA. Gag targets tRNALys for viral packaging through Gag s interaction with LysRS a tRNALys-binding protein while reverse transcriptase RT sequences within GagPol the thumb domain bind to tRNALys. The further annealing of tRNALys3 to viral RNA requires nucleocapsid NC sequences in Gag but not the NC sequences GagPol. In this report we further show that while the RT connection domain in GagPol is not required for tRNALys3 packaging into the virus it is required for tRNALys3 annealing to .
