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.
Mutational analysis of the cysteine-rich region of the iron-responsive GATA factor Fep1. Role of individual cysteines as [2Fe–2S] cluster ligands / BONACCORSI DI PATTI, Maria Carmela; Cutone, Antimo; Musci, Giovanni. - In: CELL BIOCHEMISTRY AND BIOPHYSICS. - ISSN 1085-9195. - 76:3(2018), pp. 339-344. [10.1007/s12013-018-0842-9]
Mutational analysis of the cysteine-rich region of the iron-responsive GATA factor Fep1. Role of individual cysteines as [2Fe–2S] cluster ligands
bonaccorsi di patti maria carmela;cutone antimo;
2018
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.File | Dimensione | Formato | |
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