title: Atomic-resolution monitoring of protein maturation in live human cells by NMR.
abstract: We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms. Our approach represents a new strategy for structural investigation of endogenously expressed proteins in a physiological (cellular) environment.
authors: CERM, Magnetic Resonance Center, University of Florence, Florence, Italy. banci@cerm.unifi.it
authors: Lucia
authors: L
authors: Banci
authors: Letizia
authors: L
authors: Barbieri
authors: Ivano
authors: I
authors: Bertini
authors: Enrico
authors: E
authors: Luchinat
authors: Erica
authors: E
authors: Secci
authors: Yuguang
authors: Y
authors: Zhao
authors: A Radu
authors: AR
authors: Aricescu
mesh_terms: D002470:Cell Survival; D003300:Copper / Q000737:chemistry / Q000378:metabolism; D057809:HEK293 Cells; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D013482:Superoxide Dismutase / Q000737:chemistry* / Q000378:metabolism*; D000072105:Superoxide Dismutase-1; D015032:Zinc / Q000737:chemistry / Q000378:metabolism
chemical_list: C000606290:SOD1 protein, human; D003300:Copper; D013482:Superoxide Dismutase; D000072105:Superoxide Dismutase-1; D015032:Zinc