Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes

Autor: Ikbal Cansu Baris, Sevil Zencir, Zeki Topcu, Muge Senarisoy, Melanie J. Dobson, Gizem Caliskan, Imre Boros, Ferhan Ayaydin
Přispěvatelé: Ege Üniversitesi
Jazyk: angličtina
Rok vydání: 2017
Předmět:
0301 basic medicine
Molecular biology
transcription factor SAGA
lcsh:Medicine
Gene Expression
P300-CBP Transcription Factors
protein binding
yeast
immunoprecipitation
Biochemistry
Cell Fusion
Histones
0302 clinical medicine
Transcription (biology)
acyltransferase
Acetyltransferases/metabolism
Adaptor Proteins
Signal Transducing/metabolism

Histone Acetyltransferases/*metabolism
Humans
Protein Binding
Saccharomyces cerevisiae/*metabolism
Saccharomyces cerevisiae Proteins/*metabolism
Trans-Activators/*metabolism
Transcription Factors/metabolism
Transcriptional Activation
p300-CBP Transcription Factors/metabolism
p300-CBP Transcription Factors
lcsh:Science
transcription factor
cellular distribution
transcription initiation
Histone Acetyltransferases
Multidisciplinary
biology
histone acetyltransferase PCAF
TADA2A protein
human

Signal transducing adaptor protein
protein domain
protein function
reporter gene
3. Good health
Cell biology
Precipitation Techniques
unclassified drug
Sgf29 protein
human

TADA2B protein
human

030220 oncology & carcinogenesis
gene activity
protein protein interaction
p300-CBP-associated factor
Research Article
Cell Physiology
Apoptosis antagonizing transcription factor
Saccharomyces cerevisiae Proteins
Two-hybrid screening
DNA transcription
signal transducing adaptor protein
protein localization
Saccharomyces cerevisiae
DNA construction
DNA-binding protein
histone acetyltransferase
Article
genetic regulation
03 medical and health sciences
Acetyltransferases
complex formation
DNA-binding proteins
Saccharomyces cerevisiae protein
Genetics
alteration deficiency in activation 2 protein
Gene Regulation
controlled study
human
cell protein
Protein Interactions
Transcription factor
protein expression
Adaptor Proteins
Signal Transducing

SAGA complex
S cerevisiae

nonhuman
human cell
lcsh:R
Biology and Life Sciences
Proteins
Histone acetyltransferase
Cell Biology
alteration deficiency in activation 3 protein
Co-Immunoprecipitation
Regulatory Proteins
Research and analysis methods
apoptosis antagonizing transcription factor
enzymes and coenzymes (carbohydrates)
030104 developmental biology
Molecular biology techniques
protein analysis
Plasmid Construction
biology.protein
Trans-Activators
lcsh:Q
mammal cell
histone acetyltransferase GCN5
metabolism
transactivator protein
Transcription Factors
Zdroj: PLoS ONE
PLoS ONE, Vol 12, Iss 12, p e0189193 (2017)
ISSN: 0004-1769
2923-2376
Popis: WOS: 000417698200025
PubMed ID: 29232376
General Control Non-derepressible 5 (GCN5) and Alteration/Deficiency in Activation 2 and 3 proteins (ADA2 and ADA3, respectively) are subunits of the Histone AcetylTransferase (HAT) module of SAGA-and ATAC-type co-activators. We previously reported four new interacting partners of human ADA3 identified by screening a human fetal brain cDNA library using yeast two hybrid technology. One of these partners was Apoptosis-Antagonizing Transcription Factor (AATF), also known as Che-1, an RNA polymerase II-binding protein with a number of roles in different cellular processes including regulation of transcription, cell proliferation, cell cycle control, DNA damage responses and apoptosis. Che-1/AATF is a potential therapeutic target for cancer treatments. In this study, we aimed to identify whether besides ADA3, other components of the HAT modules of SAGA and ATAC complexes, human ADA2 and GCN5 also interact with Che-1/AATF. Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells and yeast two-hybrid assays to delineate domains in the ADA2 and GCN5 proteins required for these interactions. These findings provide new insights into the pathways regulated by ADA-containing protein complexes.
Turkish Scientific and Technological Research Assembly [112T429]; Hungarian NRDIO [GINOP-2.3.2-15-2016-00020]
This work was supported by the Turkish Scientific and Technological Research Assembly (112T429) (Dr. Sevil Zencir), and Hungarian NRDIO-GINOP-2.3.2-15-2016-00020 (Prof Imre M. Boros). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Databáze: OpenAIRE