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Eissenberg JC Shilatifard A Dorokhov N Michener DE 《Molecular genetics and genomics : MGG》2007,277(2):101-114
Phosphorylation of the large RNA Polymerase II subunit C-terminal domain (CTD) is believed to be important in promoter clearance
and for recruiting protein factors that function in messenger RNA synthesis and processing. P-TEFb is a protein kinase that
targets the (CTD). The goal of this study was to identify chromatin modifications and associations that require P-TEFb activity
in vivo. We knocked down the catalytic subunit of P-TEFb, Cdk9, in Drosophila melanogaster using RNA interference. Cdk9 knockdown flies die during metamorphosis. Phosphorylation at serine 2 and serine 5 of the CTD
heptad repeat were both dramatically reduced in knockdown larvae. Hsp 70 mRNA induction by heat shock was attenuated in Cdk9 knockdown larvae. Both mono- and trimethylation of histone H3 at lysine
4 were dramatically reduced, suggesting a link between CTD phosphorylation and histone methylation in transcribed chromatin
in vivo. Levels of the chromo helicase protein CHD1 were reduced in Cdk9 knockdown chromosomes, suggesting that CHD1 is targeted
to chromosomes through P-TEFb-dependent histone methylation. Dimethylation of histone H3 at lysine 36 was significantly reduced
in knockdown larvae, implicating CTD phosphorylation in the regulation of this chromatin modification. Binding of the RNA
Polymerase II elongation factor ELL was reduced in knockdown chromosomes, suggesting that ELL is recruited to active polymerase
via CTD phosphorylation. 相似文献
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Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription 下载免费PDF全文
Zhou M Halanski MA Radonovich MF Kashanchi F Peng J Price DH Brady JN 《Molecular and cellular biology》2000,20(14):5077-5086
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