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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. 2014 Feb 01; 457(3):391-400.BJ

Abstract

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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Authors+Show Affiliations

*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.

*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.

†Department of Molecular Biology, Plant Engineering Research Institute (PERI), Sejong University, Seoul 143-747, Republic of Korea.

*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.

*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.

*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.

*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.

*School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.

Pub Type(s)

Journal Article

Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

24206186

Citation

Kang, Hyun-Jun, et al. "A Novel Protein, Pho92, Has a Conserved YTH Domain and Regulates Phosphate Metabolism By Decreasing the mRNA Stability of PHO4 in Saccharomyces Cerevisiae." The Biochemical Journal, vol. 457, no. 3, 2014, pp. 391-400.

Kang HJ, Jeong SJ, Kim KN, et al. 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. 2014;457(3):391-400.

Kang, H. J., Jeong, S. J., Kim, K. N., Baek, I. J., Chang, M., Kang, C. M., Park, Y. S., & Yun, C. W. (2014). A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae. The Biochemical Journal, 457(3), 391-400. https://doi.org/10.1042/BJ20130862

Kang HJ, et al. 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. 2014 Feb 1;457(3):391-400. PubMed PMID: 24206186.

* Article titles in AMA citation format should be in sentence-case

TY - JOUR T1 - A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae. AU - Kang,Hyun-Jun, AU - Jeong,Sook-Jin, AU - Kim,Kyung-Nam, AU - Baek,In-Joon, AU - Chang,Miwha, AU - Kang,Chang-Min, AU - Park,Yong-Sung, AU - Yun,Cheol-Won, PY - 2013/11/12/entrez PY - 2013/11/12/pubmed PY - 2014/3/19/medline SP - 391 EP - 400 JF - The Biochemical journal JO - Biochem J VL - 457 IS - 3 N2 - 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. SN - 1470-8728 UR - https://www.unboundmedicine.com/medline/citation/24206186/A_novel_protein_Pho92_has_a_conserved_YTH_domain_and_regulates_phosphate_metabolism_by_decreasing_the_mRNA_stability_of_PHO4_in_Saccharomyces_cerevisiae_ DB - PRIME DP - Unbound Medicine ER -