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Heat shock dependent proteome changes in HEK293 chromatin proteome

ABSTRACT: Identification of proteins that associate with chromatin (fraction) upon heat shock by SILAC-based quantitative proteomics

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Gerhard Mittler

LAB HEAD: Gerhard Mittler

PROVIDER: PXD012077 | Pride | 2022-04-07

REPOSITORIES: Pride

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			Action	DRS
	CopyofListofenrichedproteinsinHS.xlsx	Xlsx
	HUMAN_HSP_RFP.fasta	Fasta
	MaxQuant_Output.zip	Other
	RitwickNuc_gb01.raw	Raw
	RitwickNuc_gb02.raw	Raw

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Publications

Heat-Shock Protein 90 Controls the Expression of Cell-Cycle Genes by Stabilizing Metazoan-Specific Host-Cell Factor HCFC1.

Antonova Aneliya A Hummel Barbara B Khavaran Ashkan A Redhaber Desiree M DM Aprile-Garcia Fernando F Rawat Prashant P Gundel Kathrin K Schneck Megan M Hansen Erik C EC Mitschke Jan J Mittler Gerhard G Miething Cornelius C Sawarkar Ritwick R

Cell reports 20191101 6

Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de novo folding in the cytosol, and this raises an important question about chaperone function in the nucleus. We performed a systematic analysis of the nuclear pool of heat-shock protein 90. Three orthogonal and independent analyses led us to the core function ...[more]

PMID: 31693902

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