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.
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.
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.
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.
C. elegans equalizes the expression of X-chromosome genes between the sexes by reducing the recruitment of RNA polymerase II to promoters of X-linked genes in hermaphrodites, using a chromosome-restructuring complex called condensin.