HIV-1 reverse transcriptase is phosphorylated in vitro and in a cellular system. NLM AIDSLINE Important note: Information in this article was accurate in 2000. The state of the art may have changed since the publication date.

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HIV-1 reverse transcriptase is phosphorylated in vitro and in a cellular system.

Int J Biochem Cell Biol. 1999 Dec;31(12):1443-52. Unique Identifier : AIDSLINE MED/20104764
Idriss H; Kawa S; Damuni Z; Thompson EB; Wilson SH; Sealy Center for Molecular Science, The University of Texas; Medical Branch Galveston, TX 77555-0851, USA. hi@st-and.ac.uk

Abstract: Phosphorylation modulates the activity of many proteins that interact with nucleic acids including DNA and RNA polymerases. The HIV-1 reverse transcriptase (RT) is essential during the replicative cycle of the HIV-1 virus. HIV-1 RT has several potential sites for phosphorylation that could regulate its activities. In this work, the phosphorylation of HIV-1 RT is examined in vitro and in vivo, to evaluate any role for this modification in regulating RT metabolism. Recombinant unphosphorylated HIV-1 RT heterodimer expressed in bacteria can be phosphorylated in vitro by several purified mammalian protein kinases. Seven kinases were tested, and five of these enzymes phosphorylated HIV-1 RT. Using an insect baculovirus expression system, the 66 kDa HIV-1 RT was also phosphorylated in vivo. However, HIV-1 RT immunoprecipitated from H9-lymphoma cells infected with HIV-1 showed negligible phosphorylation. Our results indicate that purified HIV-1 RT can be phosphorylated by several mammalian protein kinases in vitro and during expression in baculovirus infected insect cells.

Keywords: JOURNAL ARTICLE Amino Acid Sequence Animal Antibodies, Monoclonal Cell Line HIV-1 Reverse Transcriptase/*CHEMISTRY/*METABOLISM Kinetics Molecular Sequence Data Phosphates/METABOLISM Phosphorus Radioisotopes Phosphorylation Protein Kinases/*METABOLISM Recombinant Proteins/METABOLISM Spodoptera Substrate Specificity Support, Non-U.S. Gov't Support, U.S. Gov't, Non-P.H.S. Support, U.S. Gov't, P.H.S.

KWDjournalarticleaminoacidsequenceanimalantibodies,monoclonalcelllinehiv-1reversetranscriptase/KWDchemistry/KWDmetabolismkineticsmolecularsequencedataphosphates/metabolismphosphorusradioisotopesphosphorylationproteinkinases/KWDmetabolismrecombinantproteins/metabolismspodopterasubstratespecificitysupport,non-uKWDsKWDgov'tsupport,uKWDsKWDgov't,non-pKWDhKWDsKWDsupport,uKWDsKWDgov't,pKWDhKWDs
000430
A0040906

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