Synergistic activation of transcription by CBP and p53

Article Abstract:

Research suggests that the CBP transcription factor functions as a coactivator for the p53 tumour suppressor while potentiating its transcriptional activity. The CBP protein's carboxy-terminal section interacts with p53's amino-terminal activation domain in vivo and in vitro. P53's transactivation ability is destroyed by a double point mutation which also destroys its synergistic function with CBP and its binding to CBP. A multistep activation pathway could induce different functions from p53.

Tumor suppressor genes, Letter to the Editor

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Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain

Article Abstract:

The protein Tat can alter the transcription factor TFIIH-mediated carboxy-terminal domain (CTD) phosphorylation kinase activity in a way that enhances the processivity of RNA polymerase II. The HIV-1 genome codes the Tat protein due to its importance in viral replication. The TAT-stimulatory factor, the Tat-binding site RNA-binding proteins, and other related cellular cofactors also influence the Tat function.

Analysis, HIV (Viruses), HIV, Genetic regulation, Genetic transcription, Transcription (Genetics), Phosphorylation

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A tale of two tails

Article Abstract:

The link between the mechanism that make and process mRNAs is closer to explanation. Hirose and Manley have reported that the carboxy-terminal domain (CTD) is involved in the process that fashions the 3' end of the mature mRNA through cleavage and polyadenylation. Further in vitro systems could reveal detail of the process by which CTD affects splicing and capping as well a polyadenylation.

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