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Genome wide location of different components of RNA polymerase II preinitiation complex in yeast S.cerevisiae
ORGANISM(S): Saccharomyces cerevisiae 
Histone modifications regulate chromatin-dependent processes, yet the mechanisms by which they contribute to specific outcomes remain unclear. H3K4me3 is a prominent histone mark that is associated with active genes and promotes transcription through interactions with effector proteins that include ...
ORGANISM(S): Homo sapiens 
Histone modifications regulate chromatin-dependent processes, yet the mechanisms by which they contribute to specific outcomes remain unclear. H3K4me3 is a prominent histone mark that is associated with active genes and promotes transcription through interactions with effector proteins that include ...
ORGANISM(S): Homo sapiens 
Histone modifications regulate chromatin-dependent processes, yet the mechanisms by which they contribute to specific outcomes remain unclear. H3K4me3 is a prominent histone mark that is associated with active genes and promotes transcription through interactions with effector proteins that include ...
ORGANISM(S): Mus musculus 
The preinitiation complex (PIC) assembles on promoters of protein-coding genes to position RNA polymerase II (Pol II) for transcription initiation. Previous structural studies revealed the PIC on different promoters, but did not address how the PIC assembles in chromatin. In the yeast Saccharomyces ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-03-11 | PXD029840 | Pride
This SuperSeries is composed of the SubSeries listed below. Refer to individual Series
ORGANISM(S): Homo sapiens 
OFD1 is a centrosomal/basal body protein codified by a transcript that when mutated results in OFD type I (OFDI) syndrome, a pleiotropic disorders associated with ciliary dysfunction. We demonstrate that components of the Preinitiation complex of translation (PIC) colocalize to the centrosome and in...
ORGANISM(S): Mus musculus 
Requirements for preinitiation complex formation in vivo
The conserved core domain of the TATA binding protein (TBP) interacts with multiple partners forming the complexes required for transcription by RNA Polymerases I, II and III. We use genetically modified mouse embryonic fibroblasts to show that many TBP core domain mutants complement loss of endogen...
ORGANISM(S): Mus musculus 
Distinct functions of three chromatin remodelers in activator binding and preinitiation complex assembly
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