Cellular iron utilization is regulated by putative siderophore transporter FgSit1 not by free iron transporter in Fusarium graminearum

Yong Sung Park, Tae Hyoung Kim, Hyo-Ihl Chang, Ha Chin Sung, Cheol-Won Yun

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

This report investigated FgSit1, which encodes a putative ferrichrome transporter of Fusarium graminearum. The identity of the deduced amino acid sequence of FgSit1 with the amino acid sequence of ScArn1p, an FC-Fe3+ transporter of Saccharomyces cerevisiae, was 51%; both the growth defect related to the Δfet3Δarn1-4 strain of S. cerevisiae in an iron-depleted condition and the FC-Fe3+ uptake activity were recovered upon the introduction of FgSit1 into the Δfet3Δarn1-4 strain. Although ScArn1p was found in the late endosomal compartment in S. cerevisiae, FgSit1 was found on the plasma membrane in S. cerevisiae; when FgSit1 was expressed exogenously in S. cerevisiae, it showed greater FC-Fe3+ uptake activity than did ScArn1p. Additionally, in F. graminearum FC-Fe3+ uptake activity in the Δfgsit1 strain was found to be one-fourth that of the wild-type. However, Fe3+ uptake activity in the Δfgsit1 strain was 5-fold higher than that of wild-type; the gene expression of FgFtr1, a putative iron transporter, was induced by the deletion of FgSit1, but was not induced by the deletion of FgSit2. Taken together, these results strongly suggest that FgSit1 encodes a putative FC-Fe3+ transporter that mediates FC-Fe3+ uptake using a different mechanism than ScArn1p and plays an important role in the regulation of cellular iron availability in F. graminearum.

Original languageEnglish
Pages (from-to)1634-1642
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume345
Issue number4
DOIs
Publication statusPublished - 2006 Jul 14

Fingerprint

Siderophores
Fusarium
Yeast
Saccharomyces cerevisiae
Iron
Amino Acid Sequence
Ferrichrome
Amino Acids
Cell membranes
Gene expression
Cell Membrane
Availability
Gene Expression
Defects
Growth

Keywords

  • F. graminearum
  • Iron
  • S. cerevisiae
  • Siderophore
  • Transporter

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Cellular iron utilization is regulated by putative siderophore transporter FgSit1 not by free iron transporter in Fusarium graminearum. / Park, Yong Sung; Kim, Tae Hyoung; Chang, Hyo-Ihl; Sung, Ha Chin; Yun, Cheol-Won.

In: Biochemical and Biophysical Research Communications, Vol. 345, No. 4, 14.07.2006, p. 1634-1642.

Research output: Contribution to journalArticle

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abstract = "This report investigated FgSit1, which encodes a putative ferrichrome transporter of Fusarium graminearum. The identity of the deduced amino acid sequence of FgSit1 with the amino acid sequence of ScArn1p, an FC-Fe3+ transporter of Saccharomyces cerevisiae, was 51{\%}; both the growth defect related to the Δfet3Δarn1-4 strain of S. cerevisiae in an iron-depleted condition and the FC-Fe3+ uptake activity were recovered upon the introduction of FgSit1 into the Δfet3Δarn1-4 strain. Although ScArn1p was found in the late endosomal compartment in S. cerevisiae, FgSit1 was found on the plasma membrane in S. cerevisiae; when FgSit1 was expressed exogenously in S. cerevisiae, it showed greater FC-Fe3+ uptake activity than did ScArn1p. Additionally, in F. graminearum FC-Fe3+ uptake activity in the Δfgsit1 strain was found to be one-fourth that of the wild-type. However, Fe3+ uptake activity in the Δfgsit1 strain was 5-fold higher than that of wild-type; the gene expression of FgFtr1, a putative iron transporter, was induced by the deletion of FgSit1, but was not induced by the deletion of FgSit2. Taken together, these results strongly suggest that FgSit1 encodes a putative FC-Fe3+ transporter that mediates FC-Fe3+ uptake using a different mechanism than ScArn1p and plays an important role in the regulation of cellular iron availability in F. graminearum.",
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AB - This report investigated FgSit1, which encodes a putative ferrichrome transporter of Fusarium graminearum. The identity of the deduced amino acid sequence of FgSit1 with the amino acid sequence of ScArn1p, an FC-Fe3+ transporter of Saccharomyces cerevisiae, was 51%; both the growth defect related to the Δfet3Δarn1-4 strain of S. cerevisiae in an iron-depleted condition and the FC-Fe3+ uptake activity were recovered upon the introduction of FgSit1 into the Δfet3Δarn1-4 strain. Although ScArn1p was found in the late endosomal compartment in S. cerevisiae, FgSit1 was found on the plasma membrane in S. cerevisiae; when FgSit1 was expressed exogenously in S. cerevisiae, it showed greater FC-Fe3+ uptake activity than did ScArn1p. Additionally, in F. graminearum FC-Fe3+ uptake activity in the Δfgsit1 strain was found to be one-fourth that of the wild-type. However, Fe3+ uptake activity in the Δfgsit1 strain was 5-fold higher than that of wild-type; the gene expression of FgFtr1, a putative iron transporter, was induced by the deletion of FgSit1, but was not induced by the deletion of FgSit2. Taken together, these results strongly suggest that FgSit1 encodes a putative FC-Fe3+ transporter that mediates FC-Fe3+ uptake using a different mechanism than ScArn1p and plays an important role in the regulation of cellular iron availability in F. graminearum.

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