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Tuyển tập các báo cáo nghiên cứu về hóa học được đăng trên tạp chí sinh học đề tài : Phosphorylation of HIV Tat by PKR increases interaction with TAR RNA and enhances transcription | BioMed Central Virology Journal Research Open Access Phosphorylation of HIV Tat by PKR increases interaction with TAR RNA and enhances transcription Liliana Endo-Munoz1 Tammra Warby1 David Harrich2 and Nigel AJ McMillan 1 Address 1Centre for Immunology and Cancer Research University of Queensland Princess Alexandra Hospital Brisbane Australia and 2Queensland Institute of Medical Research Royal Brisbane Hospital Brisbane Australia Email Liliana Endo-Munoz - lmunoz@cicr.uq.edu.au Tammra Warby - t.warby@ugrad.unimelb.edu.au David Harrich - davidH@qimr.edu.au Nigel AJ McMillan - n.mcmillan@uq.edu.au Corresponding author Published 28 February 2005 Virology Journal 2005 2 17 doi l0.ll86 l 743-422X-2-17 Received 30 November 2004 Accepted 28 February 2005 This article is available from http www.virologyj.cOm content 2 1 17 2005 Endo-Munoz et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The interferon IFN -induced dsRNA-dependent serine threonine protein kinase PKR plays a key regulatory role in the IFN-mediated anti-viral response by blocking translation in the infected cell by phosphorylating the alpha subunit of elongation factor 2 eIF2 . The human immunodeficiency virus type 1 HIV-1 evades the anti-viral IFN response through the binding of one of its major transcriptional regulatory proteins Tat to PKR. HIV-1 Tat acts as a substrate homologue for the enzyme competing with eIF2a and inhibiting the translational block. It has been shown that during the interaction with PKR Tat becomes phosphorylated at three residues serine 62 threonine 64 and serine 68. We have investigated the effect of this phosphorylation on the function of Tat in viral transcription. HIV-1 Tat activates transcription elongation by .
