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The Eukaryotic-Specific ISD11 Is a Complex-Orphan Protein with Ability to Bind the Prokaryotic IscS

Research output: Contribution to journalArticle

Original languageEnglish
Article numbere0157895
JournalPL o S One
DOIs
Publication statusPublished - 18 Jul 2016

Documents

  • The Eukaryotic-Specific ISD11_YAN_Accepted 7Jun2016_GOLD VoR

    The_Eukaryotic_Specific_ISD11_YAN_Accepted_7Jun2016_GOLD_VoR.pdf, 2.14 MB, application/pdf

    18/08/2016

    Final published version

    CC BY

    © 2016 Yan et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

King's Authors

Abstract

The eukaryotic protein Isd11 is a chaperone that binds and stabilizes the central component of the essential metabolic pathway responsible for formation of iron-sulfur clusters in mitochondria, the desulfurase Nfs1. Little is known about the exact role of Isd11. Here, we show that human Isd11 (ISD11) is a helical protein which exists in solution as an equilibrium between monomer, dimeric and tetrameric species when in the absence of human Nfs1 (NFS1). We also show that, surprisingly, recombinant ISD11 expressed in E. coli co-purifies with the bacterial orthologue of NFS1, IscS. Binding is weak but specific suggesting that, despite the absence of Isd11 sequences in bacteria, there is enough conservation between the two desulfurases to retain a similar mode of interaction. This knowledge may inform us on the conservation of the mode of binding of Isd11 to the desulfurase. We used evolutionary evidence to suggest Isd11 residues involved in the interaction.

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