A novel function of Aft1 in regulating ferrioxamine B uptake: Aft1 modulates Arn3 ubiquitination in Saccharomyces cerevisiae

Mi Young Jeong, Chang Min Kang, Ji Hyun Kim, Dong Hyuk Heo, Miwha Chang, In Joon Baek, Hyeong Su Ro, Il Dong Choi, Tae Hyoung Kim, Cheol-Won Yun

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Aft1 is a transcriptional activator in Saccharomyces cerevisiae that responds to iron availability and regulates the expression of genes in the iron regulon, such as FET3, FTR1 and the ARN family. Using a two-hybrid screen, we found that Aft1 physically interacts with the FOB (ferrioxamine B) transporter Arn3. This interaction modulates the ability of Arn3 to take up FOB. The interaction between Arn3 and Aft1 was confirmed by β-galactosidase, co-immunoprecipitation and SPR (surface plasmon resonance) assays. Truncated Aft1 had a stronger interaction with Arn3 and caused a higher FOB-uptake activity than full-length Aft1. Interestingly, only full-length Aft1 induced the correct localization of Arn3 in response to FOB. Furthermore, we found Aft1 affected Arn3 ubiquitination. These results suggest that Aft1 interacts with Arn3 and may regulate the ubiquitination of Arn3 in the cytosolic compartment.

Original languageEnglish
Pages (from-to)181-191
Number of pages11
JournalBiochemical Journal
Volume422
Issue number1
DOIs
Publication statusPublished - 2009 Aug 15

Fingerprint

Ubiquitination
Yeast
Saccharomyces cerevisiae
Iron
Galactosidases
Regulon
Surface Plasmon Resonance
Surface plasmon resonance
Immunoprecipitation
Assays
Genes
Availability
Gene Expression
ferrioxamine B

Keywords

  • Aft1
  • Arn3
  • Iron
  • Saccharomyces cerevisiae
  • Siderophore
  • Ubiquitination

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

A novel function of Aft1 in regulating ferrioxamine B uptake : Aft1 modulates Arn3 ubiquitination in Saccharomyces cerevisiae. / Jeong, Mi Young; Kang, Chang Min; Kim, Ji Hyun; Heo, Dong Hyuk; Chang, Miwha; Baek, In Joon; Ro, Hyeong Su; Choi, Il Dong; Kim, Tae Hyoung; Yun, Cheol-Won.

In: Biochemical Journal, Vol. 422, No. 1, 15.08.2009, p. 181-191.

Research output: Contribution to journalArticle

Jeong, MY, Kang, CM, Kim, JH, Heo, DH, Chang, M, Baek, IJ, Ro, HS, Choi, ID, Kim, TH & Yun, C-W 2009, 'A novel function of Aft1 in regulating ferrioxamine B uptake: Aft1 modulates Arn3 ubiquitination in Saccharomyces cerevisiae', Biochemical Journal, vol. 422, no. 1, pp. 181-191. https://doi.org/10.1042/BJ20082399
Jeong, Mi Young ; Kang, Chang Min ; Kim, Ji Hyun ; Heo, Dong Hyuk ; Chang, Miwha ; Baek, In Joon ; Ro, Hyeong Su ; Choi, Il Dong ; Kim, Tae Hyoung ; Yun, Cheol-Won. / A novel function of Aft1 in regulating ferrioxamine B uptake : Aft1 modulates Arn3 ubiquitination in Saccharomyces cerevisiae. In: Biochemical Journal. 2009 ; Vol. 422, No. 1. pp. 181-191.
@article{1b16cfa350ff46198b89775a7d4fc3b1,
title = "A novel function of Aft1 in regulating ferrioxamine B uptake: Aft1 modulates Arn3 ubiquitination in Saccharomyces cerevisiae",
abstract = "Aft1 is a transcriptional activator in Saccharomyces cerevisiae that responds to iron availability and regulates the expression of genes in the iron regulon, such as FET3, FTR1 and the ARN family. Using a two-hybrid screen, we found that Aft1 physically interacts with the FOB (ferrioxamine B) transporter Arn3. This interaction modulates the ability of Arn3 to take up FOB. The interaction between Arn3 and Aft1 was confirmed by β-galactosidase, co-immunoprecipitation and SPR (surface plasmon resonance) assays. Truncated Aft1 had a stronger interaction with Arn3 and caused a higher FOB-uptake activity than full-length Aft1. Interestingly, only full-length Aft1 induced the correct localization of Arn3 in response to FOB. Furthermore, we found Aft1 affected Arn3 ubiquitination. These results suggest that Aft1 interacts with Arn3 and may regulate the ubiquitination of Arn3 in the cytosolic compartment.",
keywords = "Aft1, Arn3, Iron, Saccharomyces cerevisiae, Siderophore, Ubiquitination",
author = "Jeong, {Mi Young} and Kang, {Chang Min} and Kim, {Ji Hyun} and Heo, {Dong Hyuk} and Miwha Chang and Baek, {In Joon} and Ro, {Hyeong Su} and Choi, {Il Dong} and Kim, {Tae Hyoung} and Cheol-Won Yun",
year = "2009",
month = "8",
day = "15",
doi = "10.1042/BJ20082399",
language = "English",
volume = "422",
pages = "181--191",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

TY - JOUR

T1 - A novel function of Aft1 in regulating ferrioxamine B uptake

T2 - Aft1 modulates Arn3 ubiquitination in Saccharomyces cerevisiae

AU - Jeong, Mi Young

AU - Kang, Chang Min

AU - Kim, Ji Hyun

AU - Heo, Dong Hyuk

AU - Chang, Miwha

AU - Baek, In Joon

AU - Ro, Hyeong Su

AU - Choi, Il Dong

AU - Kim, Tae Hyoung

AU - Yun, Cheol-Won

PY - 2009/8/15

Y1 - 2009/8/15

N2 - Aft1 is a transcriptional activator in Saccharomyces cerevisiae that responds to iron availability and regulates the expression of genes in the iron regulon, such as FET3, FTR1 and the ARN family. Using a two-hybrid screen, we found that Aft1 physically interacts with the FOB (ferrioxamine B) transporter Arn3. This interaction modulates the ability of Arn3 to take up FOB. The interaction between Arn3 and Aft1 was confirmed by β-galactosidase, co-immunoprecipitation and SPR (surface plasmon resonance) assays. Truncated Aft1 had a stronger interaction with Arn3 and caused a higher FOB-uptake activity than full-length Aft1. Interestingly, only full-length Aft1 induced the correct localization of Arn3 in response to FOB. Furthermore, we found Aft1 affected Arn3 ubiquitination. These results suggest that Aft1 interacts with Arn3 and may regulate the ubiquitination of Arn3 in the cytosolic compartment.

AB - Aft1 is a transcriptional activator in Saccharomyces cerevisiae that responds to iron availability and regulates the expression of genes in the iron regulon, such as FET3, FTR1 and the ARN family. Using a two-hybrid screen, we found that Aft1 physically interacts with the FOB (ferrioxamine B) transporter Arn3. This interaction modulates the ability of Arn3 to take up FOB. The interaction between Arn3 and Aft1 was confirmed by β-galactosidase, co-immunoprecipitation and SPR (surface plasmon resonance) assays. Truncated Aft1 had a stronger interaction with Arn3 and caused a higher FOB-uptake activity than full-length Aft1. Interestingly, only full-length Aft1 induced the correct localization of Arn3 in response to FOB. Furthermore, we found Aft1 affected Arn3 ubiquitination. These results suggest that Aft1 interacts with Arn3 and may regulate the ubiquitination of Arn3 in the cytosolic compartment.

KW - Aft1

KW - Arn3

KW - Iron

KW - Saccharomyces cerevisiae

KW - Siderophore

KW - Ubiquitination

UR - http://www.scopus.com/inward/record.url?scp=68749111588&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=68749111588&partnerID=8YFLogxK

U2 - 10.1042/BJ20082399

DO - 10.1042/BJ20082399

M3 - Article

C2 - 19469713

AN - SCOPUS:68749111588

VL - 422

SP - 181

EP - 191

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -