scholarly journals DNA dependent protein kinase (DNA-PK) enhances HIV transcription by promoting RNA polymerase II activity and recruitment of transcription machinery at HIV LTR

Oncotarget ◽  
2020 ◽  
Vol 11 (7) ◽  
pp. 699-726 ◽  
Author(s):  
Sonia Zicari ◽  
Adhikarimayum Lakhikumar Sharma ◽  
Geetaram Sahu ◽  
Larisa Dubrovsky ◽  
Lin Sun ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Dependent Protein Kinase ◽  
Hiv Transcription ◽  
Transcription Machinery ◽  
Dependent Protein

scholarly journals DNA-dependent protein kinase interacts functionally with the RNA polymerase II complex recruited at the human immunodeficiency virus (HIV) long terminal repeat and plays an important role in HIV gene expression

2011 ◽  
Vol 92 (7) ◽  
pp. 1710-1720 ◽  
Author(s):  
Shilpi Tyagi ◽  
Alex Ochem ◽  
Mudit Tyagi
Keyword(s):  
Gene Expression ◽  
Human Immunodeficiency Virus ◽  
Protein Kinase ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Dependent Protein Kinase ◽  
Immunodeficiency Virus ◽  
Target Sites ◽  
Dependent Protein ◽  
Rnap Ii

DNA-dependent protein kinase (DNA-PK), a nuclear protein kinase that specifically requires association with DNA for its kinase activity, plays important roles in the regulation of different DNA transactions, including transcription, replication and DNA repair, as well as in the maintenance of telomeres. Due to its large size, DNA-PK is also known to facilitate the activities of other factors by providing the docking platform at their site of action. In this study, by running several chromatin immunoprecipitation assays, we demonstrate the parallel distribution of DNA-PK with RNA polymerase II (RNAP II) along the human immunodeficiency virus (HIV) provirus before and after activation with tumour necrosis factor alpha. The association between DNA-PK and RNAP II is also long-lasting, at least for up to 4 h (the duration analysed in this study). Knockdown of endogenous DNA-PK using specific small hairpin RNAs expressed from lentiviral vectors resulted in significant reduction in HIV gene expression and replication, demonstrating the importance of DNA-PK for HIV gene expression. Sequence analysis of the HIV-1 Tat protein revealed three potential target sites for phosphorylation by DNA-PK and, by using kinase assays, we confirmed that Tat is an effective substrate of DNA-PK. Through peptide mapping, we found that two of these three potential phosphorylation sites are recognized and phosphorylated by DNA-PK. Mutational studies on the DNA-PK target sites of Tat further demonstrated the functional significance of the Tat–DNA-PK interaction. Thus, overall our results clearly demonstrate the functional interaction between DNA-PK and RNAP II during HIV transcription.

scholarly journals Stimulation of the DNA-dependent Protein Kinase by RNA Polymerase II Transcriptional Activator Proteins

1995 ◽  
Vol 270 (3) ◽  
pp. 1449-1454 ◽  
Author(s):  
Scott R. Peterson ◽  
Stephen A. Jesch ◽  
Thomas N. Chamberlin ◽  
Arik Dvir ◽  
Sridhar K. Rabindran ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcriptional Activator ◽  
Dependent Protein Kinase ◽  
Activator Proteins ◽  
Dependent Protein ◽  
Stimulation Of

scholarly journals GAL4 Is Regulated by the RNA Polymerase II Holoenzyme–Associated Cyclin-Dependent Protein Kinase SRB10/CDK8

1999 ◽  
Vol 3 (5) ◽  
pp. 673-678 ◽  
Author(s):  
Martin Hirst ◽  
Michael S Kobor ◽  
Neena Kuriakose ◽  
Jack Greenblatt ◽  
Ivan Sadowski
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Rna Polymerase Ii Holoenzyme

scholarly journals The Bur1 Cyclin-Dependent Protein Kinase Is Required for the Normal Pattern of Histone Methylation bySet2

2006 ◽  
Vol 26 (8) ◽  
pp. 3029-3038 ◽  
Author(s):  
Yaya Chu ◽  
Ann Sutton ◽  
Rolf Sternglanz ◽  
Gregory Prelich
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase Ii ◽  
Histone Methylation ◽  
Transcription Elongation ◽  
Regulatory Protein ◽  
Histone H3 ◽  
Growth Defect ◽  
Dependent Protein Kinase ◽  
General Role ◽  
Dependent Protein

ABSTRACT BUR1 and BUR2 encode the catalytic and regulatory subunits of a cyclin-dependent protein kinase complex that is essential for normal growth and has a general role in transcription elongation. To gain insight into its specific role in vivo, we identified mutations that reverse the severe growth defect of bur1Δ cells. This selection identified mutations in SET2, which encodes a histone methylase that targets lysine 36 of histone H3 and, like BUR1, has a poorly characterized role during transcription elongation. This genetic relationship indicates that SET2 activity is required for the growth defect observed in bur1Δ strains. This SET2-dependent growth inhibition occurs via methylation of histone H3 on lysine 36, since a methylation-defective allele of SET2 or a histone H3 K36R mutation also suppressed bur1Δ. We have explored the relationship between BUR1 and SET2 at the biochemical level and find that histone H3 is monomethylated, dimethylated, and trimethylated on lysine 36 in wild-type cells, but trimethylation is significantly reduced in bur1 and bur2 mutant strains. A similar methylation pattern is observed in RNA polymerase II C-terminal domain truncation mutants and in an spt16 mutant strain. Chromatin immunoprecipitation assays reveal that the transcription-dependent increase in trimethylated K36 over open reading frames is significantly reduced in bur2Δ strains. These results establish links between a regulatory protein kinase and histone methylation and lead to a model in which the Bur1-Bur2 complex counteracts an inhibitory effect of Set2-dependent histone methylation.

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