ADA (alteration/deficiency in activation) 3 is a conserved component of several transcriptional adaptor and HAT (histone acetyltransferase) complexes that regulate RNA polymerase II-mediated gene expression. Within the HAT complexes ADA3 is associated with ADA2 and the HAT GCN5 (general control non-repressed 5). ADA3 plays roles in diverse cellular processes and also in malignancies by modulating GCN5 catalytic activity and/or by interactions with other regulators. To gain a better understanding of ADA3 function, we used a yeast two-hybrid approach to screen a human fetal cDNA library for proteins that interacted with hADA3 (human ADA3). We identified three novel hADA3-interacting partners, a transcriptional regulator, AATF (apoptosis-antagonizing transcription factor), and regulatory subunits of the PP1 (protein phosphatase 1) and PP2A (protein phosphatase 2A) [PPP1R7 (PP1 regulatory subunit 7) and PPP2R5D (PP2A 56 kDa regulatory subunit δ isoform) respectively]. Analysis of truncated versions of hADA3 indicated that the C-terminal ADA2-interacting domain was not required for these interactions. Fluorescent microscopy analysis and co-immunoprecipitation provided support for the co-localization and interaction of hADA3 with these proteins in human cells. Expression of the interacting proteins altered expression of an hADA3-regulated reporter gene, suggesting functional consequences for the interactions. The detected interactions of hADA3 might extend the spectrum of mechanisms by which ADA3 can contribute to the regulation of gene expression and shed light on processes mediated by these newly identified ADA3 partners.
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Research Article|
February 15 2013
Identification of transcriptional and phosphatase regulators as interaction partners of human ADA3, a component of histone acetyltransferase complexes
Sevil Zencir;
Sevil Zencir
*Department of Medical Biology, Faculty of Medicine, Pamukkale University, Denizli 20070, Turkey
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Adam Sike;
Adam Sike
†Department of Biochemistry and Molecular Biology, Szeged University, Szeged H-6726, Hungary
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Melanie J. Dobson;
Melanie J. Dobson
‡Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, Canada B3H 4R2
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Ferhan Ayaydin;
Ferhan Ayaydin
§Cellular Imaging Laboratory, Biological Research Center, Hungarian Academy of Sciences, H-6726, Szeged, Temesvári krt. 62, Hungary
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Imre Boros;
Imre Boros
1
†Department of Biochemistry and Molecular Biology, Szeged University, Szeged H-6726, Hungary
1Correspondence may be addressed to either of these authors (email borosi@bio.u-szeged.hu or zeki.topcu@ege.edu.tr).
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Zeki Topcu
Zeki Topcu
1
¶Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, Izmir 35100, Turkey
1Correspondence may be addressed to either of these authors (email borosi@bio.u-szeged.hu or zeki.topcu@ege.edu.tr).
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Publisher: Portland Press Ltd
Received:
March 16 2012
Revision Received:
November 14 2012
Accepted:
November 20 2012
Accepted Manuscript online:
November 20 2012
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem J (2013) 450 (2): 311–320.
Article history
Received:
March 16 2012
Revision Received:
November 14 2012
Accepted:
November 20 2012
Accepted Manuscript online:
November 20 2012
Citation
Sevil Zencir, Adam Sike, Melanie J. Dobson, Ferhan Ayaydin, Imre Boros, Zeki Topcu; Identification of transcriptional and phosphatase regulators as interaction partners of human ADA3, a component of histone acetyltransferase complexes. Biochem J 1 March 2013; 450 (2): 311–320. doi: https://doi.org/10.1042/BJ20120452
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