Fungal heat shock proteins: molecular phylogenetic insights into the host takeover.
Evolutionary adaptation
Fungi
Heat shock proteins
Molecular phylogeny
Journal
Die Naturwissenschaften
ISSN: 1432-1904
Titre abrégé: Naturwissenschaften
Pays: Germany
ID NLM: 0400767
Informations de publication
Date de publication:
14 Mar 2024
14 Mar 2024
Historique:
received:
01
11
2023
accepted:
29
02
2024
revised:
26
02
2024
medline:
18
3
2024
pubmed:
14
3
2024
entrez:
14
3
2024
Statut:
epublish
Résumé
Heat shock proteins are constitutively expressed chaperones induced by cellular stress, such as changes in temperature, pH, and osmolarity. These proteins, present in all organisms, are highly conserved and are recruited for the assembly of protein complexes, transport, and compartmentalization of molecules. In fungi, these proteins are related to their adaptation to the environment, their evolutionary success in acquiring new hosts, and regulation of virulence and resistance factors. These characteristics are interesting for assessment of the host adaptability and ecological transitions, given the emergence of infections by these microorganisms. Based on phylogenetic inferences, we compared the sequences of HSP9, HSP12, HSP30, HSP40, HSP70, HSP90, and HSP110 to elucidate the evolutionary relationships of different fungal organisms to suggest evolutionary patterns employing the maximum likelihood method. By the different reconstructions, our inference supports the hypothesis that these classes of proteins are associated with pathogenic gains against endothermic hosts, as well as adaptations for phytopathogenic fungi.
Identifiants
pubmed: 38483597
doi: 10.1007/s00114-024-01903-x
pii: 10.1007/s00114-024-01903-x
doi:
Substances chimiques
Heat-Shock Proteins
0
Molecular Chaperones
0
HSP70 Heat-Shock Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
16Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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