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Article

The DNAJA2 substrate release mechanism is essential for chaperone-mediated folding.

The Journal of biological chemistry - 7 Dec 2012

Baaklini Imad, Wong Michael J H, Hantouche Christine, Patel Yogita, Shrier Alvin, Young Jason C

Abstract excerpt

DNAJA1 (DJA1/Hdj2) and DNAJA2 (DJA2) are the major J domain partners of human Hsp70/Hsc70 chaperones. Although they have overall similarity with the well characterized type I co-chaperones from yeast and bacteria, they are biologically distinct, and their functional mechanisms are poorly characterized. We identified DJA2-specific activities in luciferase folding and repression of human ether-a-go-go-related gene...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 23091061
DOI: 10.1074/jbc.M112.413278
PMCID: PMC3516741

Genes

DNAJA2
DNAJA1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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