Dataset Information

Protein S-glutathionylation in HeLa cells identified by nanoLC-LTQ-Orbitrap XL MS/MS

ABSTRACT: Cysteine modifications have been widely detected among different protein in different species. Here, we examined protein glutathionylation in HeLa cells under both untreated and diamide-treated conditions. A strategy using resin-assisted enrichment of glutathionylated proteins or peptides after biotin-switch is commonly used for detection of glutathionylation and other reversible cysteine modifications, and was also applied in this study. Using these strategies we identified a large number of glutathionylated protein with modification sites under both untreated and diamide-treated conditions.

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Hong Zhang

LAB HEAD: Sarah Perrett

PROVIDER: PXD017717 | Pride | 2020-04-29

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Sample1treatedwith10mMdiamide.msf	Msf
	Sample1treatedwith10mMdiamide.raw	Raw
	Sample1treatedwith10mMdiamide.xlsx	Xlsx
	Sample1untreated.msf	Msf
	Sample1untreated.raw	Raw

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Publications

<i>S</i>-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid.

Yang Jie J Zhang Hong H Gong Weibin W Liu Zhenyan Z Wu Huiwen H Hu Wanhui W Chen Xinxin X Wang Lei L Wu Si S Chen Chang C Perrett Sarah S

The Journal of biological chemistry 20200424 24

Heat shock protein 70 (Hsp70) proteins are a family of ancient and conserved chaperones. Cysteine modifications have been widely detected among different Hsp70 family members <i>in vivo</i>, but their effects on Hsp70 structure and function are unclear. Here, we treated HeLa cells with diamide, which typically induces disulfide bond formation except in the presence of excess GSH, when glutathionylated cysteines predominate. We show that in these cells, HspA1A (hHsp70) undergoes reversible cystei ...[more]

PMID: 32332101

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