Results 251 to 260 of about 503,680 (311)
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Two distinct mechanisms of RNA polymerase II elongation stimulation in vivo.

Molecules and Cells, 2021
Transcription by RNA polymerase II (RNA Pol II) relies on the elongation factors PAF1 complex (PAF), RTF1, and SPT6. Here, we use rapid factor depletion and multi-omics analysis to investigate how these elongation factors influence RNA Pol II elongation ...
Kristina Žumer   +6 more
semanticscholar   +1 more source

Identification of Integrator-PP2A complex (INTAC), an RNA polymerase II phosphatase

Science, 2020
Dephosphorylating RNA polymerase II Transcription in metazoans requires coordination of multiple factors to control the progression of polymerases and the integrity of their RNA products. Zheng et al.
Hai Zheng   +14 more
semanticscholar   +1 more source

The RNA Polymerase II Elongation Complex

Annual Review of Biochemistry, 1995
▪ Abstract  Synthesis of eukaryotic mRNA by RNA polymerase II is an elaborate biochemical process that requires the concerted action of a large set of transcription factors. RNA polymerase II transcription proceeds through multiple stages designated preinitiation, initiation, and elongation.
T, Aso, J W, Conaway, R C, Conaway
openaire   +3 more sources

Regulation of RNA polymerase II transcription

Current Opinion in Cell Biology, 1993
Transcription initiation plays a central role in the regulation of gene expression. Exciting developments in the last year have furthered our understanding of the interactions between general transcription factors and how these factors respond to modulators of transcription.
R, Drapkin, A, Merino, D, Reinberg
openaire   +2 more sources

Tails of RNA polymerase II

Trends in Biochemical Sciences, 1990
Eukaryotic RNA polymerase II contains two distinct structural domains: a catalytic core consisting of subunits that are homologous to other multisubunit RNA polymerases, and a unique extension of the carboxy-terminus of the largest subunit comprising tandem repeats of the seven amino acid sequence YSPTSPS. This repetitive 'tail' domain is essential for
openaire   +2 more sources

Dephosphorylating RNA polymerase II

Science, 2020
Transcription Transcription in metazoans requires coordination of multiple factors to control the progression of polymerases and the integrity of their RNA products. Zheng et al. identified a new dual-enzyme complex called INTAC, which is composed of protein phosphatase 2A (PP2A) core enzyme and the multisubunit RNA endonuclease Integrator.
openaire   +1 more source

RNA polymerase II elongation through chromatin

Nature, 2000
The machinery that transcribes protein-coding genes in eukaryotic cells must contend with repressive chromatin structures in order to find its target DNA sequences. Diverse arrays of proteins modify the structure of chromatin at gene promoters to help transcriptional regulatory proteins access their DNA recognition sites. The way in which disruption of
G, Orphanides, D, Reinberg
openaire   +2 more sources

Transcript Elongation by RNA Polymerase II

Annual Review of Biochemistry, 2010
Until recently, it was generally assumed that essentially all regulation of transcription takes place via regions adjacent to the coding region of a gene—namely promoters and enhancers—and that, after recruitment to the promoter, the polymerase simply behaves like a machine, quickly “reading the gene.” However, over the past decade a revolution in ...
Selth, L., Sigurdsson, S., Svejstrup, J.
openaire   +3 more sources

RNA polymerase II transcription cycles

Current Opinion in Genetics & Development, 1993
RNA polymerase II interacts with transcription factors to initiate the synthesis of mRNA. These interactions are cyclic, involving multiple RNA polymerase subunits and general transcription factors. Phosphorylation of the RNA polymerase II carboxyl-terminal domain may regulate these interactions.
openaire   +2 more sources

RNA Polymerase: Structural Similarities Between Bacterial RNA Polymerase and Eukaryotic RNA Polymerase II

Journal of Molecular Biology, 2000
Bacterial RNA polymerase and eukaryotic RNA polymerase II exhibit striking structural similarities, including similarities in overall structure, relative positions of subunits, relative positions of functional determinants, and structures and folding topologies of subunits.
openaire   +2 more sources

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