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, Sook Jin Jeong, Kyung Nam Kim, In Joon Baek, Miwha Chang, Chang Min Kang, Yong Sung Park, Cheol-Won Yun

Research output: Contribution to journalArticle

26 Citations (Scopus)

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 theNMD(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.

Original languageEnglish
Pages (from-to)391-400
Number of pages10
JournalBiochemical Journal
Volume457
Issue number3
DOIs
Publication statusPublished - 2014 Feb 1

Fingerprint

RNA Stability
Metabolism
Yeast
Saccharomyces cerevisiae
Phosphates
3' Untranslated Regions
Messenger RNA
Proteins
Genes
Signal transduction
Microarray Analysis
Microarrays
Half-Life
Signal Transduction
Transcription Factors
Phenotype
Degradation

Keywords

  • Pho4
  • Phosphate
  • Saccharomyces cerevisiae
  • YT521-B homology (YTH) domain
  • YTHDF2

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae. / Kang, Hyun Jun; Jeong, Sook Jin; Kim, Kyung Nam; Baek, In Joon; Chang, Miwha; Kang, Chang Min; Park, Yong Sung; Yun, Cheol-Won.

In: Biochemical Journal, Vol. 457, No. 3, 01.02.2014, p. 391-400.

Research output: Contribution to journalArticle

Kang, Hyun Jun ; Jeong, Sook Jin ; Kim, Kyung Nam ; Baek, In Joon ; Chang, Miwha ; Kang, Chang Min ; Park, Yong Sung ; Yun, Cheol-Won. / A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae. In: Biochemical Journal. 2014 ; Vol. 457, No. 3. pp. 391-400.
@article{f6d255dc895347ee8290f10efc630062,
title = "A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae",
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 theNMD(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.",
keywords = "Pho4, Phosphate, Saccharomyces cerevisiae, YT521-B homology (YTH) domain, YTHDF2",
author = "Kang, {Hyun Jun} and Jeong, {Sook Jin} and Kim, {Kyung Nam} and Baek, {In Joon} and Miwha Chang and Kang, {Chang Min} and Park, {Yong Sung} and Cheol-Won Yun",
year = "2014",
month = "2",
day = "1",
doi = "10.1042/BJ20130862",
language = "English",
volume = "457",
pages = "391--400",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

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 - 2014/2/1

Y1 - 2014/2/1

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 theNMD(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.

AB - 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 theNMD(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.

KW - Pho4

KW - Phosphate

KW - Saccharomyces cerevisiae

KW - YT521-B homology (YTH) domain

KW - YTHDF2

UR - http://www.scopus.com/inward/record.url?scp=84892164576&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84892164576&partnerID=8YFLogxK

U2 - 10.1042/BJ20130862

DO - 10.1042/BJ20130862

M3 - Article

VL - 457

SP - 391

EP - 400

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -