TY  - GEN
A1  - Yan, Robert
A1  - Friemel, Martin
A1  - Aloisi, Claudia
A1  - Huynen, Martijn
A1  - Taylor, Ian A.
A1  - Leimkühler, Silke
A1  - Pastore, Annalisa
T1  - The eukaryotic-specific Isd11 is a complex- orphan protein with ability to bind the prokaryotic IscS
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - 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.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 551 
KW  - sulfur cluster formation
KW  - Escherichia coli
KW  - cysteine desulfurase
KW  - interacting protein
KW  - bacterial frataxin
KW  - statistical-model
KW  - biogenesis
KW  - biosynthesis
KW  - NFS1
KW  - deficiency
Y1  - 2019
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/41190
UR  - https://nbn-resolving.org/urn:nbn:de:kobv:517-opus4-411906
SN  - 1866-8372
IS  - 551
ER  -