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Transcription elongation factor A

The protein encoded by this gene is found in the nucleus, where it functions as an SII class transcription elongation factor. Elongation factors in this class are responsible for releasing RNA polymerase II ternary complexes from transcriptional arrest at template-encoded arresting sites. The encoded protein has been shown to interact with general transcription factor IIB, a basal transcription factor. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: POLYMERASE, CAN, p105, ACID, Histone
Papers on TFIIS
TFIIS-Dependent Non-coding Transcription Regulates Developmental Genome Rearrangements.
Nowak et al., Warsaw, Poland. In Plos Genet, Jul 2015
To understand how ncRNAs are produced from the entire genome, we have focused on a homolog of the TFIIS elongation factor, which regulates RNA polymerase II transcriptional pausing.
Ccr4-Not and TFIIS Function Cooperatively To Rescue Arrested RNA Polymerase II.
Reese et al., United States. In Mol Cell Biol, Jul 2015
Here we describe how Ccr4-Not and TFIIS cooperate to stimulate elongation.
Sequence features and transcriptional stalling within centromere DNA promote establishment of CENP-A chromatin.
Allshire et al., Edinburgh, United Kingdom. In Plos Genet, Mar 2015
Cells lacking factors involved in restarting transcription-TFIIS and Ubp3-assemble CENP-ACnp1 on central domain DNA when CENP-ACnp1 is at wild-type levels, suggesting that persistent stalling of RNAPII on centromere DNA triggers chromatin remodelling events that deposit CENP-ACnp1.
Analysis of the transgenerational iron deficiency stress memory in Arabidopsis thaliana plants.
Morandini et al., Milano, Italy. In Front Plant Sci, 2014
The frequency of somatic homologous recombination (SHR) events, of DNA strand breaks as well as the expression of the transcription elongation factor TFIIS-like gene increase when plants are grown under Fe deficiency.
A genetic assay for transcription errors reveals multilayer control of RNA polymerase II fidelity.
Strathern et al., Frederick, United States. In Plos Genet, 2014
The mutations are in three domains of Rpb1, the trigger loop, the bridge helix, and in sites involved in binding to TFIIS.
Crystal structure of the 14-subunit RNA polymerase I.
Müller et al., 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.
Maraia et al., 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.
RNF20-RNF40: A ubiquitin-driven link between gene expression and the DNA damage response.
Oren et al., Tel Aviv-Yafo, Israel. In Febs Lett, 2011
New evidence indicates that the regulatory function of H2Bub on gene expression can selectively enhance or suppress the expression of distinct subsets of genes through a mechanism involving the hPAF1 complex and the TFIIS protein.
DNA damage response and transcription.
Mullenders et al., 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.
Structural basis of RNA polymerase II backtracking, arrest and reactivation.
Cramer et al., München, Germany. In Nature, 2011
Arrested Pol II is reactivated by transcription factor IIS (TFIIS), which induces RNA cleavage that is required for cell viability.
The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS.
Roeder et al., New York City, United States. In Cell, 2010
Importantly, we further demonstrate a strong synergy between hPAF1C and elongation factor SII/TFIIS and an underlying mechanism involving direct hPAF1C-SII interactions and cooperative binding to RNA polymerase II.
Structure-function analysis of RNA polymerases I and III.
Soutourina et al., 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.
[Mechanisms of action of RNA polymerase-binding transcription factors that do not bind to DNA].
Severinov et al., In Biofizika, 2009
A class of transcription factors, including the prokaryotic proteins GreA, GreB, Gfh1, Rnk, DksA, and TraR and eukaryotic TFIIS, that do not bind DNA but directly interact wth RNA polymerase have been considered.
Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution.
Kornberg et al., Stanford, United States. In Science, 2009
The predominant mechanism of proofreading is the excision of a dinucleotide in the presence of the elongation factor SII (TFIIS).
RNA polymerase I: a multifunctional molecular machine.
Pikaard et al., 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.
RNA polymerase II bypasses 8-oxoguanine in the presence of transcription elongation factor TFIIS.
Tanaka et al., Suita, Japan. In Dna Repair (amst), 2007
SII is important for preventing cellular death due to oxidative DNA damage, assisting RNAPII to bypass 8-oxoG
A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS.
Landick et al., Madison, United States. In Proc Natl Acad Sci U S A, 2005
data suggest that because TFIIS promotes escape from promoter-proximal pauses by stimulating cleavage of back-tracked nascent RNA, TFIIS inhibition may help DSIF/NELF negatively regulate productive transcription
Efficient release from promoter-proximal stall sites requires transcript cleavage factor TFIIS.
Lis et al., Ithaca, United States. In Mol Cell, 2005
TFIIS is critical for efficient release of Pol II from the hsp70 promoter region
RNA polymerase II complexes in the very early phase of transcription are not susceptible to TFIIS-induced exonucleolytic cleavage.
Timmers et al., Utrecht, Netherlands. In Nucleic Acids Res, 2002
RNA polymerase II complexes in the very early phase of transcription are not susceptible to TFIIS-induced exonucleolytic cleavage.
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