Crystal structure of the 14-subunit RNA polymerase I.
Madrid, Spain. In Nature, 2013
Subunit A12.2 extends from the A190 jaw to the active site and inserts a transcription elongation factor TFIIS-like zinc ribbon into the nucleotide triphosphate entry pore, providing insight into the role of A12.2 in RNA cleavage and Pol I insensitivity to α-amanitin.
Transcription termination by the eukaryotic RNA polymerase III.
Bethesda, United States. In Biochim Biophys Acta, 2013
While pol III termination is autonomous involving the core subunits C2 and probably C1, it also involves subunits C11, C37 and C53, which act on the pol III catalytic center and exhibit homology to the pol II elongation factor TFIIS and TFIIFα/β respectively.
DNA damage response and transcription.
Leiden, Netherlands. In Dna Repair (amst), 2011
CSB functions as a repair coupling factor to attract NER proteins, chromatin remodelers and the CSA-E3-ubiquitin ligase complex to the stalled RNAPIIo; CSA is dispensable for attraction of NER proteins, yet in cooperation with CSB is required to recruit XAB2, the nucleosomal binding protein HMGN1 and TFIIS.
Structure-function analysis of RNA polymerases I and III.
France. In Curr Opin Struct Biol, 2009
Unexpectedly, even though Pol I and III, but not Pol II, have an intrinsic RNA cleavage activity, it was found that TFIIS Pol II cleavage stimulation factor also played a general role in Pol III transcription.
RNA polymerase I: a multifunctional molecular machine.
Saint Louis, United States. In Cell, 2008
Their study reveals that three subunits of Pol I perform functions in transcription elongation that are outsourced to the transcription factors TFIIF and TFIIS in the analogous Pol II transcription system.