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Identification of nucleosome assembly protein 1 (NAP1) as an interacting partner of plant ribosomal protein S6 (RPS6) and a positive regulator of rDNA transcription

Authors
Son, OraKim, SunghanShin, Yun-jeongKim, Woo-YoungKoh, Hee-JongCheon, Choong-Ill
Issue Date
Sep-2015
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Ribosomal protein S6; Histone deacetylase 2B; Nucleosome assembly protein 1; TOR; rDNA transcription
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.465, no.2, pp 200 - 205
Pages
6
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
465
Number
2
Start Page
200
End Page
205
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/10247
DOI
10.1016/j.bbrc.2015.07.150
ISSN
0006-291X
1090-2104
Abstract
The ribosomal protein S6 (RPS6) is a downstream component of the signaling mediated by the target of rapamycin (TOR) kinase that acts as a central regulator of the key metabolic processes, such as protein translation and ribosome biogenesis, in response to various environmental cues. In our previous study, we identified a novel role of plant RPS6, which negatively regulates rDNA transcription, forming a complex with a plant-specific histone deacetylase, AtHD2B. Here we report that the Arabidopsis RPS6 interacts additionally with a histone chaperone, nucleosome assembly protein 1(AtNAP1;1). The interaction does not appear to preclude the association of RPS6 with AtHD2B, as the AtNAP1 was also able to interact with AtHD2B as well as with an RPS6-AtHD2B fusion protein in the BiFC assay and pulldown experiment. Similar to a positive effect of the ribosomal S6 kinase 1 (AtS6K1) on rDNA transcription observed in this study, overexpression or down regulation of the AtNAP1;1 resulted in concomitant increase and decrease, respectively, in rDNA transcription suggesting a positive regulatory role played by AtNAP1 in plant rDNA transcription, possibly through derepression of the negative effect of the RPS6-AtHD2B complex. (C) 2015 Elsevier Inc. All rights reserved.
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