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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Biochemical characterization of HIV-1 Rev as a potent activator of casein kinase II in vitro.

The stimulatory effects of several DNA-binding basic proteins (histone and protamine) and HIV-1 Rev with arginine (Arg)-rich clusters on the activity of casein kinase II ( CK-II) were investigated in vitro. It was found that recombinant Rev (rRev) and the synthetic oligo-fragments corresponding to the amino acid sequences of its Arg-rich cluster stimulate CK-II activity in a dose-dependent manner. The activated CK-II phosphorylates several cellular and viral proteins in HIV-1 infected human MOLT-4 cells, and also phosphorylates HIV-1 structural proteins, including recombinant reverse transcriptase (rRT). These phosphorylations are selectively inhibited by CK-II inhibitors, such as quercetin, oGA (a glycyrrhetinic acid derivative) and NCS-chrom (an enediyne containing antibiotic). The data presented here suggest that HIV-1 Rev acts as an effective potent activator of CK-II, which may be a cellular mediator promoting HIV-1 replication in virus-infected cells.[1]

References

  1. Biochemical characterization of HIV-1 Rev as a potent activator of casein kinase II in vitro. Ohtsuki, K., Maekawa, T., Harada, S., Karino, A., Morikawa, Y., Ito, M. FEBS Lett. (1998) [Pubmed]
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