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Significance Transcriptional elongation by RNA polymerase II produces full-length RNA transcripts and plays a general and prominent role in regulating gene expression. The positive transcription elongation factor b (P-TEFb) is one of the most important transcription factors controlling this process. The core P-TEFb, consisting of cyclin-dependent kinase 9 and cyclin T (CycT), exists in a network of complexes that include the 7SK small nuclear ribonucleoprotein particle (7SK snRNP), the super elongation complexes (SECs), and the bromodomain protein 4 (Brd4)–P-TEFb complex. This study identifies AF4/FMR2 family member 1 (AFF1) as a ubiquitous binding partner of core P-TEFb throughout the entire P-TEFb network. By increasing the affinity of the HIV-encoded transactivating (Tat) protein for CycT1, AFF1 is required for Tat’s extraction of P-TEFb from 7SK snRNP and the formation of SECs for maximal HIV transcriptional activation.

AFF1 is a ubiquitous P-TEFb partner to enable Tat extraction of P-TEFb from 7SK snRNP and formation of SECs for HIV transactivation