Structure-function analysis of the super elongation complex formed when HIV replicates inside cells reveals that the HIV-1 Tat protein binds to a cleft between P-TEFb, an enzyme that is involved in normal transcription, and AFF4, a protein that is used to build the super elongation complex
Transcription elongation by the elongation factor P-TEFb promotes the epithelial–mesenchymal transition and metastasis of breast cancer cells, implicating inhibition of this factor as a potential treatment for the late stages of this cancer.
TRIM28 was found to be a versatile dual-function latency contributor by bridging both suppressive epigenetic modifications and RNAP II transcriptional-pausing, and can be a novel target to develop latency-reversing agents.
Acetylation of the circadian transcription factor BMAL1 by the acetyltransferase TIP60 is crucial for recruitment of the pause release factors to clock gene promoters and productive elongation of these genes.
While the transcription factor c-Myc explores the space in the nucleus in an unrestricted manner, the elongation factor P-TEFb's sampling of the nucleus is constrained to a complex domain with fractal characteristics.