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

Gizem Caliskan, Ikbal C. Baris, F. Ayaydin, Melanie J. Dobson, Muge Senarisoy, I. Boros, Zeki Topcu, Sevil Zencir

Research output: Article

1 Citation (Scopus)

Abstract

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.

Original languageEnglish
Article numbere0189193
JournalPLoS One
Volume12
Issue number12
DOIs
Publication statusPublished - dec. 1 2017

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Histone Acetyltransferases
Transcription Factors
apoptosis
transcription factors
Apoptosis
Yeast
Proteins
proteins
Cells
two hybrid system techniques
Two-Hybrid System Techniques
Oncology
Cell proliferation
Transcription
DNA-directed RNA polymerase
Cell Cycle Checkpoints
Gene Library
Immunoprecipitation
cDNA libraries
DNA damage

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Cite this

Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes. / Caliskan, Gizem; Baris, Ikbal C.; Ayaydin, F.; Dobson, Melanie J.; Senarisoy, Muge; Boros, I.; Topcu, Zeki; Zencir, Sevil.

In: PLoS One, Vol. 12, No. 12, e0189193, 01.12.2017.

Research output: Article

Caliskan, Gizem ; Baris, Ikbal C. ; Ayaydin, F. ; Dobson, Melanie J. ; Senarisoy, Muge ; Boros, I. ; Topcu, Zeki ; Zencir, Sevil. / Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes. In: PLoS One. 2017 ; Vol. 12, No. 12.
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abstract = "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.",
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