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Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli.

Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. Research Abstract Details 

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  • Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. Abstract Text:

    umechiyo tokumotoUmechiyo Tokumoto,shinobu nomuraShinobu Nomura,yoshiko minamiYoshiko Minami,hisaaki miharaHisaaki Mihara,shin-ichiro katoShin-Ichiro Kato,tatsuo kuriharaTatsuo Kurihara,nobuyoshi esakiNobuyoshi Esaki,hiroshi kanazawaHiroshi Kanazawa,hiroshi matsubaraHiroshi Matsubara,yasuhiro takahashiYasuhiro Takahashi,

    The assembly of iron-sulfur (Fe-S) clusters is mediated by complex machinery which, in Escherichia coli, is encoded by the iscRSUA-hscBA-fdx-ORF3 gene cluster. Here, we demonstrate the network of protein-protein interactions among the components involved in the machinery. We have constructed (His)(6)-tagged versions of the components and identified their interacting partners that were co-purified from E. coli extracts with a Ni-affinity column. Direct associations of the defined pair of proteins were further examined in yeast cells using the two-hybrid system. In accord with the previous in vitro binding and kinetic experiments, interactions were observed for the combinations of IscS and IscU, IscU and HscB, IscU and HscA, and HscB and HscA. In addition, we have identified previously unreported interactions between IscS and Fdx, IscS and ORF3, IscA and HscA, and HscA and Fdx. We also found, by site-directed mutational analysis combined with the two-hybrid system, that two cysteine residues in IscU are essential for binding with HscB but not with IscS. Despite the complex network of interactions in various combinations of components, heteromultimeric complexes were not observed in our experiments except for the putative oligomeric form of IscU-IscS-ORF3. Thus, the sequential association and dissociation among the IscS, IscU, IscA, HscB, HscA, Fdx, and ORF3 proteins may be a critical process in the assembly of Fe-S clusters.

    Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. Publishing Authors By Initials

    u tokumotoU Tokumoto,s nomuraS Nomura,y minamiY Minami,h miharaH Mihara,s katoS Kato,t kuriharaT Kurihara,n esakiN Esaki,h kanazawaH Kanazawa,h matsubaraH Matsubara,y takahashiY Takahashi,

    For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research

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    Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 131

    Page Numbers: 713-9

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: May

    YEAR: 2002

    Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. Keywords Mesh Terms:

    KEYWORDS: beta-Galactosidase

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. Information

    Substance Name: beta-Galactosidase

    Registry Number: EC 3.2.1.23

    Grant and Affiliation Information for Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli.

    AFFILIATION: Department of Biology, Graduate School of Science, Osaka University, Machikaneyama, Toyonaka, Osaka 560-0043, Japan.

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: J Biochem

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