In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1

被引：52

作者：

Banci, Lucia ^{[1
,2
]}

Barbieri, Letizia ^{[1
,2
]}

Bertini, Ivano ^{[1
,2
]}

Cantini, Francesca ^{[1
,2
]}

Luchinat, Enrico ^{[1
,2
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr, Sesto Fiorentino, Italy

[2] Univ Florence, Dept Chem, Sesto Fiorentino, Italy

来源：

PLOS ONE | 2011年 / 6卷 / 08期

关键词：

AMYOTROPHIC-LATERAL-SCLEROSIS; MITOCHONDRIAL INTERMEMBRANE SPACE; ESCHERICHIA-COLI; REDUCED FORM; COPPER; SOD1; DISMUTASE; METAL; SPECTROSCOPY; APO;

D O I：

10.1371/journal.pone.0023561

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

In-cell NMR allows characterizing the folding state of a protein as well as posttranslational events at molecular level, in the cellular context. Here, the initial maturation steps of human copper, zinc superoxide dismutase 1 are characterized in the E. coli cytoplasm by in-cell NMR: from the apo protein, which is partially unfolded, to the zinc binding which causes its final quaternary structure. The protein selectively binds only one zinc ion, whereas in vitro also the copper site binds a non-physiological zinc ion. However, no intramolecular disulfide bridge formation occurs, nor copper uptake, suggesting the need of a specific chaperone for those purposes.

引用

页数：8

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