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Int J Biochem Cell Biol. 1999 Dec;31(12):1443-52.

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

Author information

1
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.

PMID:
10641798
DOI:
10.1016/s1357-2725(99)00097-7
[Indexed for MEDLINE]

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