The eukaryotic-specific Isd11 is a complex- orphan protein with ability to bind the prokaryotic IscS
- 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.
Author details: | Robert Yan, Martin Friemel, Claudia Aloisi, Martijn HuynenORCiD, Ian A. Taylor, Silke LeimkühlerORCiDGND, Annalisa Pastore |
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URN: | urn:nbn:de:kobv:517-opus4-411906 |
DOI: | https://doi.org/10.25932/publishup-41190 |
ISSN: | 1866-8372 |
Title of parent work (English): | Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe |
Publication series (Volume number): | Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (551) |
Publication type: | Postprint |
Language: | English |
Date of first publication: | 2019/01/28 |
Publication year: | 2016 |
Publishing institution: | Universität Potsdam |
Release date: | 2019/01/28 |
Tag: | NFS1; bacterial frataxin; biogenesis; biosynthesis; cysteine desulfurase; deficiency; interacting protein; statistical-model; sulfur cluster formation Escherichia coli |
Issue: | 551 |
Number of pages: | 14 |
Source: | PLOS ONE 11 (2016) 7, Art. e0157895 DOI 10.1371/journal.pone.0157895 |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät |
DDC classification: | 5 Naturwissenschaften und Mathematik / 50 Naturwissenschaften / 500 Naturwissenschaften und Mathematik |
6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit | |
Peer review: | Referiert |
Publishing method: | Open Access |
Grantor: | Public Library of Science (PLOS) |
License (German): | CC-BY - Namensnennung 4.0 International |