Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II C-terminal domain.

Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II C-terminal domain.

Nucleic Acids Res. 1996 Feb 1;24(3):501-8. Unique Identifier : AIDSLINE MED/96173650
Herrmann CH; Gold MO; Rice AP; Division of Molecular Virology, Baylor College of Medicine,; Houston, TX 77030, USA.

Abstract: Phosphorylation of the carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II has been implicated as an important step in transcriptional regulation. Previously, we reported that a cellular CTD kinase, TAK, is targeted by the human immunodeficiency virus transactivator Tat. In the present study, we analyzed several other transactivators for the ability to interact with CTD kinases in vitro. The adenovirus E1A and herpes simplex virus VP16 proteins, but not other transactivators tested, were found to associate with a cellular kinase activity that hyperphosphorylates the CTD. The interaction is dependent upon a functional activation domain of E1A or VP16, suggesting that the interaction with a CTD kinase is relevant for the transactivation function of these proteins. The CTD kinase activities that interact with E1A and VP16 are related to each other but distinct from TAK. The Tat-, E1A- and VP16-associated CTD kinase activities detected in our assay also appear unrelated to MO15, the catalytic component of the CTD kinase activity of the general transcription factor TFIIH. Thus, this study has identified a novel interaction between viral transactivators and a cellular CTD kinase and suggests that at least two CTD kinases may mediate responses to viral transactivators.

Keywords: Adenovirus E1A Proteins/*METABOLISM Base Sequence Hela Cells Herpes Simplex Virus Protein Vmw65/*METABOLISM Human Molecular Sequence Data Phosphorylation Protein Kinases/*METABOLISM RNA Polymerase II/*METABOLISM Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Trans-Activators/*METABOLISM JOURNAL ARTICLE
960730
M9670421

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