• search hit 43 of 993
Back to Result List

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.

Download full text files

  • pmnr551.pdfeng
    (2289KB)

    SHA-1: 7489b7f8af7fd7edcc7f7b0bcfdebde13bd5f190

Export metadata

Additional Services

Share in Twitter Search Google Scholar Statistics
Metadaten
Author:Robert Yan, Martin Friemel, Claudia Aloisi, Martijn HuynenORCiD, Ian A. Taylor, Silke Leimkühler, Annalisa Pastore
URN:urn:nbn:de:kobv:517-opus4-411906
DOI:https://doi.org/10.25932/publishup-41190
ISSN:1866-8372
Parent Title (English):Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
Series (Serial Number):Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (551)
Document Type:Postprint
Language:English
Date of first Publication:2019/01/28
Year of Completion: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
Pagenumber:14
Source:PLOS ONE 11 (2016) 7, Art. e0157895 DOI 10.1371/journal.pone.0157895
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät
Dewey Decimal 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
Publication Way:Open Access
Grantor:Public Library of Science (PLOS)
Licence (German):License LogoCreative Commons - Namensnennung, 4.0 International