The homologue of human YTHDF2, Ydr374c (Pho92), is the only protein that has a YTH (YT521-B homology) domain in Saccharomyces cerevisiae. Based on microarray analysis, genes involved in the phosphate signal transduction (PHO) pathway were up-regulated in the Δpho92 strain, as were genes regulated by Pho4, which is an important transcription factor in the PHO pathway. To identify the exact mechanism of Pho92 action with respect to phosphate metabolism, we investigated the effect of Pho92 on PHO4 expression. The half-life of PHO4 mRNA was increased in the Δpho92 strain; this phenotype was also observed in the deletion mutants UPF1 and POP2, which are components of the NMD (nonsense-mediated decay) pathway and the Pop2–Ccr4–Not deadenylase complex respectively. Pho92 interacts physically with Pop2 of the Pop2–Ccr4–Not deadenylase complex. Furthermore, Pho92 binding to the 3′-UTR of PHO4 was dependent on the phosphate concentration. Deletion of the PHO4 3′-UTR resulted in PHO4 mRNA resistance to Pho92-dependent degradation. The results of the present study indicate that Pho92 regulates Pho4 expression at the post-transcriptional level via the regulation of mRNA stability. Taken together, Pho92 participates in cellular phosphate metabolism, specifically via the regulation of PHO4 mRNA stability by binding to the 3′-UTR in a phosphate-dependent manner.
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Research Article|
January 10 2014
A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae
Hyun-Jun Kang;
Hyun-Jun Kang
*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea
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Sook-Jin Jeong;
Sook-Jin Jeong
*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea
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Kyung-Nam Kim;
Kyung-Nam Kim
†Department of Molecular Biology, Plant Engineering Research Institute (PERI), Sejong University, Seoul 143-747, Republic of Korea
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In-Joon Baek;
In-Joon Baek
*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea
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Miwha Chang;
Miwha Chang
*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea
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Chang-Min Kang;
Chang-Min Kang
*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea
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Yong-Sung Park;
Yong-Sung Park
*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea
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Cheol-Won Yun
Cheol-Won Yun
1
*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea
1To whom correspondence should be addressed (email cheolwony@korea.ac.kr).
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Publisher: Portland Press Ltd
Received:
July 01 2013
Revision Received:
October 29 2013
Accepted:
November 08 2013
Accepted Manuscript online:
November 08 2013
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem J (2014) 457 (3): 391–400.
Article history
Received:
July 01 2013
Revision Received:
October 29 2013
Accepted:
November 08 2013
Accepted Manuscript online:
November 08 2013
Citation
Hyun-Jun Kang, Sook-Jin Jeong, Kyung-Nam Kim, In-Joon Baek, Miwha Chang, Chang-Min Kang, Yong-Sung Park, Cheol-Won Yun; A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae. Biochem J 1 February 2014; 457 (3): 391–400. doi: https://doi.org/10.1042/BJ20130862
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