Mutational Analysis of the Cysteine-Rich Region of the Iron-Responsive GATA Factor Fep1. Role of Individual Cysteines as [2Fe-2S] Cluster Ligands

Cell Biochemistry and Biophysics
Maria Carmela Bonaccorsi di PattiGiovanni Musci

Abstract

Fep1, the iron-dependent GATA-type transcriptional repressor of the methylotrophic yeast Pichia pastoris, has a dimeric structure and binds an iron-sulfur cluster of the [2Fe-2S] type. In this work, we extend the characterization of this protein by analysis of the optical and CD spectroscopic properties of a set of mutants where cysteines within the conserved Cys-X5-Cys-X8-Cys-X2-Cys motif have been targeted, in order to evaluate their role as [2Fe-2S] ligands. The results suggest that all four cysteine residues are essential because replacing them with serines in different combinations invariably produces a protein unable to correctly bind the [2Fe-2S] cluster.

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Citations

Aug 23, 2019·Genome Génome / Conseil National De Recherches Canada·Mina YuYongfeng Liu
Jan 6, 2021·European Biophysics Journal : EBJ·Adriana E MieleMaria Carmela Bonaccorsi di Patti
Dec 13, 2019·Inorganic Chemistry·Iogann TolbatovAlessandro Marrone
Sep 28, 2020·Biochimica Et Biophysica Acta. Bioenergetics·Carsten BerndtUlrich Mühlenhoff
Oct 13, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Matthias MisslingerHubertus Haas

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Methods Mentioned

BETA
circular dichroism

Software Mentioned

DichroWeb
SWISS
MODEL

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