title: Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20.
abstract: Iron-sulfur (Fe-S) clusters are inorganic cofactors that are fundamental to several biological processes in all three kingdoms of life. In most organisms, Fe-S clusters are initially assembled on a scaffold protein, ISCU, and subsequently transferred to target proteins or to intermediate carriers by a dedicated chaperone/co-chaperone system. The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins, and, in mammals, it relies on the activity of a multiprotein transfer complex that contains the chaperone HSPA9, the co-chaperone HSC20 and the scaffold ISCU. How the transfer complex efficiently engages recipient Fe-S target proteins involves specific protein interactions that are not fully understood. This mini review focuses on recent insights into the molecular mechanism of amino acid motif recognition and discrimination by the co-chaperone HSC20, which guides Fe-S cluster delivery.
authors.affiliation: Molecular Medicine Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, 9000 Rockville Pike, 20892 Bethesda, MD, USA. rouault@mail.nih.gov.
authors.forename: N
authors.initials: N
authors.lastname: Maio
authors.affiliation: Molecular Medicine Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, 9000 Rockville Pike, 20892 Bethesda, MD, USA. rouault@mail.nih.gov.
authors.forename: T A
authors.initials: TA
authors.lastname: Rouault
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D006801:Humans; D007506:Iron-Sulfur Proteins / Q000032:analysis / Q000378:metabolism*; D018832:Molecular Chaperones / Q000032:analysis / Q000378:metabolism*; D011485:Protein Binding; D060066:Protein Interaction Maps
chemical_list: C490651:HSCB protein, human; D007506:Iron-Sulfur Proteins; D018832:Molecular Chaperones