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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.

SUBMITTER: Banci L

PROVIDER: S-EPMC4017183 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Atomic-resolution monitoring of protein maturation in live human cells by NMR.

Banci Lucia L Barbieri Letizia L Bertini Ivano I Luchinat Enrico E Secci Erica E Zhao Yuguang Y Aricescu A Radu AR

Nature chemical biology 20130303 5

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 physiolo ...[more]

PMID: 23455544

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