The tandem SH2 domains of Spt6 use novel mechanisms to bind unexpected phosphorylated serine and threonine residues in the RNA polymerase II linker to recruit Spt6 to sites of transcription and maintain repressive chromatin.

Genome-wide analysis reveals novel functions for a post-translational modification to the carboxy-terminal domain (CTD) of RNA Polymerase II in mammals.

The requirements for preinitiation complex formation/stability and transcription by RNA polymerase II in yeast cells are different from those in vitro, thereby altering the current view of basal transcription.

Histone variant H2A.Z is deposited near transcription start sites by the chromatin remodeler SWR1 and seems to be removed by RNA polymerase II at an early stage of transcription elongation.

Lysine mono- and di-methylation are two novel post-translational modifications of RNA polymerase II, which are enriched at promoters of active genes, precede lysine acetylation and mark early stages of transcription.

Quantification of all the major on- and off-pathway kinetic parameters in the transcription elongation cycle reveals that RNA polymerase II translocates slowly in a linear, non-branched Brownian ratchet mechanism.

Quantitative super resolution imaging, in live mammalian cells, reveals a direct relationship between protein clustering dynamics and the number of mRNA transcribed at an endogenous gene locus.

Tat uses unexpected regulatory mechanisms to reprogram target immune cells to promote viral replication and rewire pathways beneficial for HIV.

The ATP-dependent chromatin remodeler Chd1 controls nucleosome turnover to allow RNA Polymerase to transcribe in vivo.

CDK9 inhibition in human cells uncovers that Pol II pause duration regulates the frequency of productive transcription initiation.