Balk, J., Pierik, A. J., Aguilar Netz, D. J., Mühlenhoff, U. and Lill, R. (2005) Nar1p, a conserved eukaryotic protein with similarity to Fe-only hydrogenases, functions in cytosolic iron-sulphur protein biogenesis. Biochemical Society Transactions, 33 (1). pp. 86-89. ISSN 0300-5127
Full text not available from this repository. (Request a copy)Abstract
The genome of the yeast Saccharomyces cerevisiae encodes the essential protein Nar1p that is conserved in virtually all eukaryotes and exhibits striking sequence similarity to bacterial iron-only hydrogenases. Previously, we have shown that Nar1p is an Fe-S protein and that assembly of its co-factors depends on the mitochondrial Fe-S cluster biosynthesis apparatus. Using functional studies in vivo, we demonstrated that Nar1p has an essential role in the maturation of cytosolic and nuclear, but not of mitochondrial, Fe-S proteins. Here we provide further spectroscopic evidence that Nar1p possesses two Fe-S clusters. We also show that Nar1p is required for Fe-S cluster assembly on the P-loop NTPase Nbp35p, another newly identified component of the cytosolic Fe-S protein assembly machinery. These data suggest a complex biochemical pathway of extra-mitochondrial Fe-S protein biogenesis involving unique eukaryotic proteins.
Item Type: | Article |
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Faculty \ School: | Faculty of Science > School of Biological Sciences |
UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Molecular Microbiology |
Depositing User: | Rhiannon Harvey |
Date Deposited: | 07 Feb 2012 15:51 |
Last Modified: | 10 Aug 2023 16:30 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/36917 |
DOI: | 10.1042/BST0330086 |
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