ArticleMolecular plant pathology2023
Insight into the biochemical and cell biological function of an intrinsically unstructured heat shock protein, Hsp12 of Ustilago maydis.
Article in Molecular plant pathology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 9 citations in OpenAlex.
- Core virome shapes adaptation of a phytopathogenic fungus to climate and cropping patterns.The ISME journal · 2026Article
- Crowding in Anhydrobiosis.Sub-cellular biochemistry · 2025Review
- The role of membrane physiology in sHSP Lo18-lipid interaction and lipochaperone activity.Scientific reports · 2024Article
- The EH domain-containing protein, EdeA, is involved in endocytosis, cell wall integrity, and pathogenicity inmSphere · 2024Article
- Fungal heat shock proteins: molecular phylogenetic insights into the host takeover.Die Naturwissenschaften · 2024Article
- Insight into the biochemical and cell biological function of an intrinsically unstructured heat shock protein, Hsp12 of Ustilago maydis.Molecular plant pathology · 2023Article
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Authors and funding
7 authors at 1 institution in 1 country.
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Abstract
Small heat shock proteins (sHsps) play diverse roles in the stress response and maintenance of cellular functions. The Ustilago maydis genome codes for few sHsps. Among these, Hsp12 has previously been demonstrated to be involved in the pathogenesis of the fungus by our group. In the present study we further investigated the biological function of the protein in the pathogenic development of U. maydis. Analysis of the primary amino acid sequence of Hsp12 in combination with spectroscopic methods to analyse secondary protein structures revealed an intrinsically disordered nature of the protein. We also carried out detailed analysis on the protein aggregation prevention activity associated with Hsp12. Our data suggest Hsp12 has trehalose-dependent protein aggregation prevention activity. Through assaying the interaction of Hsp12 with lipid membranes in vitro we also showed the ability of U. maydis Hsp12 to induce stability in lipid vesicles. U. maydis hsp12 deletion mutants exhibited defects in the endocytosis process and delayed completion of the pathogenic life cycle. Therefore, U. maydis Hsp12 contributes to the pathogenic development of the fungus through its ability to relieve proteotoxic stress during infection as well as its membrane-stabilizing function.
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