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

We used NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We could follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 (CCS) oxidation of t...

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Autores principales: Banci, Lucia, Barbieri, Letizia, Bertini, Ivano, Luchinat, Enrico, Secci, Erica, Zhao, Yuguang, Aricescu, A. Radu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017183/
https://www.ncbi.nlm.nih.gov/pubmed/23455544
http://dx.doi.org/10.1038/nchembio.1202
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author Banci, Lucia
Barbieri, Letizia
Bertini, Ivano
Luchinat, Enrico
Secci, Erica
Zhao, Yuguang
Aricescu, A. Radu
author_facet Banci, Lucia
Barbieri, Letizia
Bertini, Ivano
Luchinat, Enrico
Secci, Erica
Zhao, Yuguang
Aricescu, A. Radu
author_sort Banci, Lucia
collection PubMed
description We used NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We could follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 (CCS) oxidation of the SOD1 intrasubunit disulfide bond occurs through both copper-dependent and independent mechanisms. Our approach represents a new strategy for structural investigation of endogeneously expressed proteins within a physiological (cellular) environment.
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spelling pubmed-40171832014-05-12 Atomic-resolution monitoring of protein maturation in live human cells by NMR Banci, Lucia Barbieri, Letizia Bertini, Ivano Luchinat, Enrico Secci, Erica Zhao, Yuguang Aricescu, A. Radu Nat Chem Biol Article We used NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We could follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 (CCS) oxidation of the SOD1 intrasubunit disulfide bond occurs through both copper-dependent and independent mechanisms. Our approach represents a new strategy for structural investigation of endogeneously expressed proteins within a physiological (cellular) environment. 2013-03-03 2013-05 /pmc/articles/PMC4017183/ /pubmed/23455544 http://dx.doi.org/10.1038/nchembio.1202 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Banci, Lucia
Barbieri, Letizia
Bertini, Ivano
Luchinat, Enrico
Secci, Erica
Zhao, Yuguang
Aricescu, A. Radu
Atomic-resolution monitoring of protein maturation in live human cells by NMR
title Atomic-resolution monitoring of protein maturation in live human cells by NMR
title_full Atomic-resolution monitoring of protein maturation in live human cells by NMR
title_fullStr Atomic-resolution monitoring of protein maturation in live human cells by NMR
title_full_unstemmed Atomic-resolution monitoring of protein maturation in live human cells by NMR
title_short Atomic-resolution monitoring of protein maturation in live human cells by NMR
title_sort atomic-resolution monitoring of protein maturation in live human cells by nmr
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017183/
https://www.ncbi.nlm.nih.gov/pubmed/23455544
http://dx.doi.org/10.1038/nchembio.1202
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