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DAXX represents a new type of protein-folding enabler
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Journal Article
DAXX represents a new type of protein-folding enabler
2021
Overview
Protein quality control systems are crucial for cellular function and organismal health. At present, most known protein quality control systems are multicomponent machineries that operate via ATP-regulated interactions with non-native proteins to prevent aggregation and promote folding
1
, and few systems that can broadly enable protein folding by a different mechanism have been identified. Moreover, proteins that contain the extensively charged poly-Asp/Glu (polyD/E) region are common in eukaryotic proteomes
2
, but their biochemical activities remain undefined. Here we show that DAXX, a polyD/E protein that has been implicated in diverse cellular processes
3
–
10
, possesses several protein-folding activities. DAXX prevents aggregation, solubilizes pre-existing aggregates and unfolds misfolded species of model substrates and neurodegeneration-associated proteins. Notably, DAXX effectively prevents and reverses aggregation of its in vivo-validated client proteins, the tumour suppressor p53 and its principal antagonist MDM2. DAXX can also restore native conformation and function to tumour-associated, aggregation-prone p53 mutants, reducing their oncogenic properties. These DAXX activities are ATP-independent and instead rely on the polyD/E region. Other polyD/E proteins, including ANP32A and SET, can also function as stand-alone, ATP-independent molecular chaperones, disaggregases and unfoldases. Thus, polyD/E proteins probably constitute a multifunctional protein quality control system that operates via a distinctive mechanism.
A protein chaperone system is identified that consists of proteins with poly-Asp/Glu sequence, and may have an important role in diseases characterized by protein aggregation.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 13/106
/ 13/109
/ 13/89
/ 13/95
/ 14/19
/ 14/28
/ 38/79
/ 45/77
/ 45/90
/ 82/83
/ 96
/ Animals
/ Co-Repressor Proteins - metabolism
/ E region
/ Folding
/ Humanities and Social Sciences
/ Humans
/ Molecular Chaperones - metabolism
/ Mutation
/ Peptides
/ Protein Aggregation, Pathological - prevention & control
/ Proteins
/ Proteostasis Deficiencies - prevention & control
/ Proto-Oncogene Proteins c-mdm2 - chemistry
/ Proto-Oncogene Proteins c-mdm2 - metabolism
/ Science
/ Tumor Suppressor Protein p53 - chemistry
/ Tumor Suppressor Protein p53 - genetics
/ Tumor Suppressor Protein p53 - metabolism
/ Tumors
