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Cat No | BPA-16718 |
Conjugate | |
Type | Methylated Antibody |
Source | Rabbit |
Size | 50 uL |
Application | WB; IHC; IF |
Format | Liquid |
Concentration | Please refer to the vial lable for the specific concentration. |
Buffer | Supplied in PBS with 0.02% sodium azide,50% glycerol,pH7.3. |
Species | Human |
Storage | Store at -20℃. Avoid freeze / thaw cycles. |
Synonyms | H3.4;H3/g;H3FT;H3t;HIST3H3;Histone H3;HIST1H3A |
Purification | Affinity purification |
MolecularWeight | 17KDa |
Description | |
Background | Actin is a key regulator of RNA polymerase (Pol) II-dependent transcription. Positive transcription elongation factor b (P-TEFb), a Cdk9/cyclin T1 heterodimer, has been reported to play a critical role in transcription elongation. However, the relationship between actin and P-TEFb is still not clear. In this study, actin was found to interact with Cdk9, a catalytic subunit of P-TEFb, in elongation complexes. Using immunofluorescence and immunoprecipitation assays, Cdk9 was found to bind to G-actin through the conserved Thr-186 in the T-loop. Overexpression and in vitro kinase assays showed that G-actin promotes P-TEFb-dependent phosphorylation of the Pol II C-terminal domain. An in vitro transcription experiment revealed that the interaction between G-actin and Cdk9 stimulated Pol II transcription elongation. ChIP and immobilized template assays indicated that actin recruited Cdk9 to a transcriptional template in vivo and in vitro. Using cytokine IL-6-inducible p21 gene expression system, we revealed that actin recruited Cdk9 to endogenous gene. Moreover, overexpression of actin and Cdk9 increased histone H3 acetylation and acetylized histone H3 binding to a transcriptional template through the interaction with histone acetyltransferase, p300. Taken together, our results suggested that actin participates in transcription elongation by recruiting Cdk9 for phosphorylation of the Pol II C-terminal domain, and the actin-Cdk9 interaction promotes chromatin remodeling. |