Nuclear fate of yeast snoRNA is determined by co-transcriptional Rnt1 cleavage.

Small nucleolar RNA (snoRNA) are conserved and essential non-coding RNA that are transcribed by RNA Polymerase II (Pol II). Two snoRNA classes, formerly distinguished by their structure and ribonucleoprotein composition, act as guide RNA to target RNA such as ribosomal RNA, and thereby introduce specific modifications. We have studied the 5'end processing of individually transcribed snoRNA in S.

The integrator complex recognizes a new double mark on the RNA polymerase II carboxyl-terminal domain.

The carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II (pol II) comprises multiple tandem repeats of the heptapeptide Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7). This unusual structure serves as a platform for the binding of factors required for expression of pol II-transcribed genes, including the small nuclear RNA (snRNA) gene-specific Integrator complex. The pol II CTD specifically mediates recruitment of Integrator to the promoter of snRNA genes to activate transcription and direct 3' end processing of the transcripts.

Bisphosphonate mRNA cap analog attached to Sepharose for affinity chromatography of decapping enzymes.

m(7)GTP-Sepharose is routinely used for cap binding protein isolation. Here we present the synthesis of a new affinity resin containing a mononucleotide cap analog resistant to hydrolysis by DcpS. The resin has been designed in order to identify and purify Arabidopsis thaliana DcpS and other pyrophosphatases.