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.
Atomic-resolution monitoring of protein maturation in live human cells by NMR / BANCI, LUCIA; BARBIERI, LETIZIA; BERTINI, IVANO; LUCHINAT, ENRICO; SECCI, ERICA; Zhao Y; Aricescu AR. - In: NATURE CHEMICAL BIOLOGY. - ISSN 1552-4450. - ELETTRONICO. - 9:(2013), pp. 297-299. [10.1038/NCHEMBIO.1202]
Atomic-resolution monitoring of protein maturation in live human cells by NMR
LUCHINAT, ENRICO;
2013
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
