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Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions

PLoS biology, 2010-04, Vol.8 (4), p.e1000354-e1000354 [Peer Reviewed Journal]

Shi et al. 2010 ;2010 Shi 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: Shi R, Proteau A, Villarroya M, Moukadiri I, Zhang L, et al. (2010) Structural Basis for Fe-S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein-Protein Interactions. PLoS Biol 8(4): e1000354. doi:10.1371/journal.pbio.1000354 ;ISSN: 1545-7885 ;ISSN: 1544-9173 ;EISSN: 1545-7885 ;DOI: 10.1371/journal.pbio.1000354 ;PMID: 20404999

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Title:
Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions
Author: Shi, Rong ; Proteau, Ariane ; Villarroya, Magda ; Moukadiri, Ismaïl ; Zhang, Linhua ; Trempe, Jean-François ; Matte, Allan ; Armengod, M Eugenia ; Cygler, Miroslaw
Petsko, Gregory A.
Subjects: Biochemistry/Macromolecular Assemblies and Machines ; Biosynthesis ; Carbon-Sulfur Lyases - chemistry ; Carbon-Sulfur Lyases - genetics ; Carbon-Sulfur Lyases - metabolism ; Catalytic Domain ; Cell Biology/Microbial Growth and Development ; Crystallography, X-Ray ; Enzymes ; Escherichia coli - genetics ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Iron ; Iron-Sulfur Proteins - chemistry ; Iron-Sulfur Proteins - genetics ; Iron-Sulfur Proteins - metabolism ; Medical research ; Microbiology ; Microbiology/Microbial Growth and Development ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Proteins ; RNA, Transfer - chemistry ; RNA, Transfer - metabolism ; Sulfhydryl Compounds - chemistry ; Sulfur - chemistry ; Sulfur - metabolism
Is Part Of: PLoS biology, 2010-04, Vol.8 (4), p.e1000354-e1000354
Description: The cysteine desulfurase IscS is a highly conserved master enzyme initiating sulfur transfer via persulfide to a range of acceptor proteins involved in Fe-S cluster assembly, tRNA modifications, and sulfur-containing cofactor biosynthesis. Several IscS-interacting partners including IscU, a scaffold for Fe-S cluster assembly; TusA, the first member of a sulfur relay leading to sulfur incorporation into the wobble uridine of several tRNAs; ThiI, involved in tRNA modification and thiamine biosynthesis; and rhodanese RhdA are sulfur acceptors. Other proteins, such as CyaY/frataxin and IscX, also bind to IscS, but their functional roles are not directly related to sulfur transfer. We have determined the crystal structures of IscS-IscU and IscS-TusA complexes providing the first insight into their different modes of binding and the mechanism of sulfur transfer. Exhaustive mutational analysis of the IscS surface allowed us to map the binding sites of various partner proteins and to determine the functional and biochemical role of selected IscS and TusA residues. IscS interacts with its partners through an extensive surface area centered on the active site Cys328. The structures indicate that the acceptor proteins approach Cys328 from different directions and suggest that the conformational plasticity of a long loop containing this cysteine is essential for the ability of IscS to transfer sulfur to multiple acceptor proteins. The sulfur acceptors can only bind to IscS one at a time, while frataxin and IscX can form a ternary complex with IscU and IscS. Our data support the role of frataxin as an iron donor for IscU to form the Fe-S clusters.
Publisher: United States: Public Library of Science
Language: English
Identifier: ISSN: 1545-7885
ISSN: 1544-9173
EISSN: 1545-7885
DOI: 10.1371/journal.pbio.1000354
PMID: 20404999
Source: PLoS (Open access)
GFMER Free Medical Journals
MEDLINE
PubMed Central
ProQuest Central
DOAJ Directory of Open Access Journals

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Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions

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