scholarly journals LncRNA GA-Binding Protein Transcription Factor Subunit Beta-1 Antisense RNA 1 Inhibits Renal Carcinoma Growth Through an MiR-1246/Phosphoenolpyruvate Carboxykinase 1 Pathway

2020 ◽  
Vol Volume 13 ◽  
pp. 6827-6836
Author(s):  
Shuang Gao ◽  
Feng Zhang ◽  
Hanxue Sun ◽  
Xianghong Yang
Keyword(s):  
Transcription Factor ◽  
Antisense Rna ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Renal Carcinoma ◽  
Binding Protein ◽  
Ga Binding Protein ◽  
Protein Transcription

scholarly journals Human Lineage-Specific Transcriptional Regulation through GA-Binding Protein Transcription Factor Alpha (GABPa)

2016 ◽  
Vol 33 (5) ◽  
pp. 1231-1244 ◽  
Author(s):  
Alvaro Perdomo-Sabogal ◽  
Katja Nowick ◽  
Ilaria Piccini ◽  
Ralf Sudbrak ◽  
Hans Lehrach ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcriptional Regulation ◽  
Binding Protein ◽  
Human Lineage ◽  
Factor Alpha ◽  
Ga Binding Protein ◽  
Protein Transcription

scholarly journals Identification of GA-Binding Protein Transcription Factor Alpha Subunit (GABPA) as a Novel Bookmarking Factor

2019 ◽  
Vol 20 (5) ◽  
pp. 1093 ◽  
Author(s):  
Shunya Goto ◽  
Masashi Takahashi ◽  
Narumi Yasutsune ◽  
Sumiki Inayama ◽  
Dai Kato ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Histone Acetylation ◽  
Binding Protein ◽  
Alpha Subunit ◽  
Upstream Region ◽  
G1 Phase ◽  
Sp1 Transcription Factor ◽  
Factor Alpha ◽  
Ga Binding Protein ◽  
Protein Transcription

Mitotic bookmarking constitutes a mechanism for transmitting transcriptional patterns through cell division. Bookmarking factors, comprising a subset of transcription factors (TFs), and multiple histone modifications retained in mitotic chromatin facilitate reactivation of transcription in the early G1 phase. However, the specific TFs that act as bookmarking factors remain largely unknown. Previously, we identified the “early G1 genes” and screened TFs that were predicted to bind to the upstream region of these genes, then identified GA-binding protein transcription factor alpha subunit (GABPA) and Sp1 transcription factor (SP1) as candidate bookmarking factors. Here we show that GABPA and multiple histone acetylation marks such as H3K9/14AC, H3K27AC, and H4K5AC are maintained at specific genomic sites in mitosis. During the M/G1 transition, the levels of these histone acetylations at the upstream regions of genes bound by GABPA in mitosis are decreased. Upon depletion of GABPA, levels of histone acetylation, especially H4K5AC, at several gene regions are increased, along with transcriptional induction at 1 h after release. Therefore, we proposed that GABPA cooperates with the states of histone acetylation to act as a novel bookmarking factor which, may negatively regulate transcription during the early G1 phase.

scholarly journals Functional Interactions of Transcription Factor Human GA-binding Protein Subunits

1998 ◽  
Vol 273 (45) ◽  
pp. 29302-29308 ◽  
Author(s):  
Fumihiko Suzuki ◽  
Masahide Goto ◽  
Chika Sawa ◽  
Seiichiro Ito ◽  
Hajime Watanabe ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Binding Protein ◽  
Protein Subunits ◽  
Functional Interactions ◽  
Ga Binding Protein

scholarly journals TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation

1997 ◽  
Vol 324 (1) ◽  
pp. 249-253 ◽  
Author(s):  
Jean M. RAWLING ◽  
Rafael ALVAREZ-GONZALEZ
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase Ii ◽  
Binding Protein ◽  
Polymerase Activity ◽  
Tata Binding Protein ◽  
Covalent Modification ◽  
Eukaryotic Transcription ◽  
Calf Thymus ◽  
Associated Proteins ◽  
Protein Transcription

We have examined the susceptibility of some of the basal eukaryotic transcription factors as covalent targets for poly(ADP-ribosyl)ation. Human recombinant TATA-binding protein, transcription factor (TF)IIB and TFIIF (made up of the 30 and 74 kDa RNA polymerase II-associated proteins RAP30 and RAP74) were incubated with calf thymus poly(ADP-ribose) polymerase and [32P]NAD+ at 37 °C. On lithium dodecyl sulphate/PAGE and autoradiography, two bands of radioactivity, coincident with RAP30 and RAP74, were observed. No radioactivity co-migrated with TATA-binding protein or TFIIB. The phenomenon was dependent on the presence of nicked DNA, which is essential for poly(ADP-ribose) polymerase activity. Covalent modification of TFIIF increased with time of incubation, with increasing TFIIF concentration and with increasing NAD+ concentration. High-resolution PAGE confirmed that the radioactive species associated with RAP30 and RAP74 were ADP-ribose polymers. From these observations, we conclude that both TFIIF subunits are highly specific substrates for covalent poly(ADP-ribosyl)ation.

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