ArticleProtein science : a publication of the Protein Society2026
ATP modulates holdase activity of fungal and human 110-kilodalton heat shock proteins to promote protein folding.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- ATP modulates holdase activity of fungal and human 110-kilodalton heat shock proteins to promote protein folding.Protein science : a publication of the Protein Society · 2026Article
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7 authors.
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Abstract
Heat shock proteins of the 70-kDa family (Hsp70s) are highly abundant and conserved molecular chaperones that help preserve proteostasis primarily by facilitating proper protein folding. Heat shock protein of the 110-kDa family (Hsp110s), a specialized branch of the Hsp70/Hsp110 superfamily, function both as nucleotide exchange factor (NEF) cochaperones for Hsp70s and as independent "holdase" chaperones that stabilize non-native polypeptides to prevent aggregation and facilitate downstream refolding by Hsp70s. While Hsp110 NEF activity is well characterized, the consequences of adenosine 5'-triphosphate (ATP) binding for Hsp110 holdase behavior have remained largely unexplored. Although holdase activity is generally considered nucleotide-independent, reports of ATP-dependent effects have raised questions about the underlying mechanism. Here, we examined the biochemical properties of Multicopy Suppressor of ira1 3 (Msi3), the sole Hsp110 in Candida albicans, to dissect the role of ATP in holdase function. We first identified an inhibitory effect of elevated Mg
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