Conservation of Aconitase Residues Revealed by Multiple Sequence Analysis

Implications for Structure/Function Relationships

Authors

  • Dmitrij Frishman,

    1. European Molecular Biology Laboratory, Heidelberg, Germany
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  • Matthias W. Hentze

    Corresponding author
    1. European Molecular Biology Laboratory, Heidelberg, Germany
      M. W. Hentze, Cytoplasmic Gene regulation, European Molecular Biology Laboratory, Postfach 102209, Meyerhofstrasse 1, D-69012 Heidelberg, Germany
      Fax: +49 6221 387510.
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  • Supplementary material.Conservation of aconitase revealed by multiple sequence analysis. Implications for structure/funcation relationships.Fig. S1. Multiple alignment of the Fe-S isomearse sequences built by the program CLUSTAL W. This information is available upon request from the Editorial Office.

M. W. Hentze, Cytoplasmic Gene regulation, European Molecular Biology Laboratory, Postfach 102209, Meyerhofstrasse 1, D-69012 Heidelberg, Germany
Fax: +49 6221 387510.

Abstract

Aconitases have recently regained much attention, because one member of this family, iron regulatory protein-1 (IRP-1), has been found to play a dual role as a cytoplasmic aconitase and a regulatory RNA-binding protein. This finding has highlighted a novel role for Fe-S clusters as post-translational regulatory switches. We have aligned 28 members of the Fe-S isomerase family, identified highly conserved amino acid residues, and integrated this information with data on the crystallographic structure of mammalian mitochondrial aconitase. We propose structural and/or functional roles for the previously unrecognized conserved residues. Our findings illustrate the value of detailed protein sequence analysis when high-resolution crystallographic data are already available.

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