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Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. Zusätzlich bieten wir Ihnen Transcription Elongation Factor SPT5 Antikörper (51) und Transcription Elongation Factor SPT5 Proteine (7) und viele weitere Produktgruppen zu diesem Protein an.
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The mobile C-terminal region of DSIF is located near exiting RNA, where it can recruit factors for RNA processing.
OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1beta (zeige TRIM28 ELISA Kits), and a purified OGA-SPT5-TIF1beta (zeige TRIM28 ELISA Kits) complex has elongation properties.
A transcription-independent effect of tumor necrosis factor alpha on RNA splicing, mediated by Spt5.
SPT5 contributes to the up-regulation of hTERT expression and colonic tumor development.
Data indicate that the Plus3 domain of the Rtf1 (zeige RTF1 ELISA Kits) subunit mediates Paf1C recruitment to genes by binding a repeating domain within the phosphorylated elongation factor Spt5.
DSIF Is Selectively Required for mRNA Splicing and Export of NF-kappaB (zeige NFKB1 ELISA Kits) Target Genes.
RNA polymerase II elongation repression is critically dependent on the C-terminus of Spt5
crystal structure of hSpt4 in complex with the dimerization region of hSpt5
phosphorylated by P-TEFb (zeige CCNT1 ELISA Kits) kinase during HIV-1 transcription in Tat (zeige TAT ELISA Kits)/TAR (zeige RBM8A ELISA Kits) dependent manner
hSpt5 function in transcription regulation and mRNA capping is essential for a subset of cellular and viral genes and may not be required for global gene expression.
Spt5 accumulation at variable genes distinguishes somatic hypermutation in germinal center B cells from ex vivo-activated cells.
our findings indicate that Spt4 and Spt5 have essential functions in the DNA repair phase of immunoglobulin class switch recombination.
Study reports that Spt5, a factor normally associated with stalled or paused Pol II, is required for class switch recombination.
The phosphorylation of SPT5 by CDKD;2 enables it to recruit VIP5 to regulate chromatin and transcription in Arabidopsis.
SPT5-like protein emerged in plants as a facultative RNA polymerase elongation factor.[SPT5]
the positive function of Foggy/Spt5 is required for gata1 (zeige GATA1 ELISA Kits) expression during zebrafish embryonic hematopoiesis.
The elongation factors Pandora/Spt6 and Foggy/Spt5 promote transcription in the zebrafish embryo.
spt 5-dependent transcript elongation is required cell-autonomously for a complex cell migration
Spt5 as a dual regulator of transcription elongation in vivo; a small but diverse set of target genes critically dependent on Spt5 during development.
Mutation in the protein-protein interaction domain (REPO domain) of Pho interferes with the dynamics of its interaction with Spt5. The transcriptional kinetics of the heat shock response is negatively affected by a mutation in the REPO domain of Pho
Spt5 interacts both physically and genetically with the Polycomb Group (PcG) protein Pleiohomeotic (Pho)
We show that SPT5 interacts directly with MSL1 in vitro and is required downstream of MSL complex recruitment, providing the first mechanistic data corroborating the elongation model of dosage compensation.
Spt5 acts both positively and negatively on transcription in vivo during heat shock induction.
Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV- 1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences.
DRB sensitivity-inducing factor 160 kDa subunit
, DRB sensitivity-inducing factor large subunit
, DSIF large subunit
, DSIF p160
, Tat-cotransactivator 1 protein
, transcription elongation factor SPT5
, suppressor of Ty 5 homolog
, transcription elongation factor Spt5
, transcription elongation factor spt5
, protein foggy
, transcription elongation regulator foggy
, Chromatin elongation factor SPT5