Phosphorylation of tyrosine 1 in the carboxy-terminal domain (CTD) of the largest subunit of RNA Polymerase (RNAP) II functions to stabilize this domain, and facilitates turnover of upstream antisense RNAs.

The yeast mRNA decapping enzyme Dcp1/Dcp2 repressses many genes whose products are required on poor carbon or nitrogen sources in nutrient-replete cells by mRNA decapping and degradation or translational repression, adding post-transcriptional controls to the transcriptional repression of these functions.

The natural compounds cordycepin and mycophenolic acid stimulate alternative polyadenylation through opposing effects on transcriptional rate.

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.

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.

Dhh1, Pat1, and Lsm1 target subsets of cellular mRNAs for decapping via interactions of these regulatory proteins with the C-terminal domain of Dcp2, the catalytic component of the decapping enzyme.

The SPARC complex directs accurate RNAPII positioning for transcription initiation and, in some instances, ensures correct transcription directionality in Trypanosoma brucei.

A novel pair of isobaric crosslinking reagents is described, which allow relative quantification of crosslinker-modified peptides during mass spectrometry analysis for comparative structural studies of proteins and protein complexes.

Genome-wide recruitment of Mediator and Pol II is reduced in yeast lacking the Med2-Med3-Med15 tail module triad, and Mediator association with gene promoters depends on Pol II, Taf1, and TBP.

Transient DNA interactions by DNA-binding proteins are utilized by herpes simple virus as an alternative route to generate membraneless compartments in the nucleus without invoking phase separation.