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Diversity and evolution of chitin synthases in oomycetes (Straminipila: Oomycota).
Mol Phylogenet Evol. 2019 10; 139:106558.MP

Abstract

The oomycetes are filamentous eukaryotic microorganisms, distinct from true fungi, many of which act as crop or fish pathogens that cause devastating losses in agriculture and aquaculture. Chitin is present in all true fungi, but it occurs in only small amounts in some Saprolegniomycetes and it is absent in Peronosporomycetes. However, the growth of several oomycetes is severely impacted by competitive chitin synthase (CHS) inhibitors. Here, we shed light on the diversity, evolution and function of oomycete CHS proteins. We show by phylogenetic analysis of 93 putative CHSs from 48 highly diverse oomycetes, including the early diverging Eurychasma dicksonii, that all available oomycete genomes contain at least one putative CHS gene. All gene products contain conserved CHS motifs essential for enzymatic activity and form two Peronosporomycete-specific and six Saprolegniale-specific clades. Proteins of all clades, except one, contain an N-terminal microtubule interacting and trafficking (MIT) domain as predicted by protein domain databases or manual analysis, which is supported by homology modelling and comparison of conserved structural features from sequence logos. We identified at least three groups of CHSs conserved among all oomycete lineages and used phylogenetic reconciliation analysis to infer the dynamic evolution of CHSs in oomycetes. The evolutionary aspects of CHS diversity in modern-day oomycetes are discussed. In addition, we observed hyphal tip rupture in Phytophthora infestans upon treatment with the CHS inhibitor nikkomycin Z. Combining data on phylogeny, gene expression, and response to CHS inhibitors, we propose the association of different CHS clades with certain developmental stages.

Authors+Show Affiliations

KTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Chemistry, Division of Glycoscience, AlbaNova University Centre, 100 44 Stockholm, Sweden.KTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Chemistry, Division of Glycoscience, AlbaNova University Centre, 100 44 Stockholm, Sweden; ARC Centre of Excellence in Plant Cell Walls and School of Agriculture, Food and Wine, The University of Adelaide, Waite Campus, Urrbrae, SA 5064, Australia. Electronic address: bulone@kth.se.Department of Mathematics, Stockholm University, Swedish e-Science Research Centre, Science for Life Laboratory, 106 91 Stockholm, Sweden. Electronic address: arve@math.su.se.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

31288106

Citation

Klinter, Stefan, et al. "Diversity and Evolution of Chitin Synthases in Oomycetes (Straminipila: Oomycota)." Molecular Phylogenetics and Evolution, vol. 139, 2019, p. 106558.
Klinter S, Bulone V, Arvestad L. Diversity and evolution of chitin synthases in oomycetes (Straminipila: Oomycota). Mol Phylogenet Evol. 2019;139:106558.
Klinter, S., Bulone, V., & Arvestad, L. (2019). Diversity and evolution of chitin synthases in oomycetes (Straminipila: Oomycota). Molecular Phylogenetics and Evolution, 139, 106558. https://doi.org/10.1016/j.ympev.2019.106558
Klinter S, Bulone V, Arvestad L. Diversity and Evolution of Chitin Synthases in Oomycetes (Straminipila: Oomycota). Mol Phylogenet Evol. 2019;139:106558. PubMed PMID: 31288106.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Diversity and evolution of chitin synthases in oomycetes (Straminipila: Oomycota). AU - Klinter,Stefan, AU - Bulone,Vincent, AU - Arvestad,Lars, Y1 - 2019/07/06/ PY - 2018/04/06/received PY - 2019/07/05/revised PY - 2019/07/05/accepted PY - 2019/7/10/pubmed PY - 2020/3/7/medline PY - 2019/7/10/entrez KW - Chitin synthase KW - Evolution KW - Growth inhibition KW - Microtubule interacting and trafficking (MIT) domain KW - Oomycete KW - Phylogeny SP - 106558 EP - 106558 JF - Molecular phylogenetics and evolution JO - Mol. Phylogenet. Evol. VL - 139 N2 - The oomycetes are filamentous eukaryotic microorganisms, distinct from true fungi, many of which act as crop or fish pathogens that cause devastating losses in agriculture and aquaculture. Chitin is present in all true fungi, but it occurs in only small amounts in some Saprolegniomycetes and it is absent in Peronosporomycetes. However, the growth of several oomycetes is severely impacted by competitive chitin synthase (CHS) inhibitors. Here, we shed light on the diversity, evolution and function of oomycete CHS proteins. We show by phylogenetic analysis of 93 putative CHSs from 48 highly diverse oomycetes, including the early diverging Eurychasma dicksonii, that all available oomycete genomes contain at least one putative CHS gene. All gene products contain conserved CHS motifs essential for enzymatic activity and form two Peronosporomycete-specific and six Saprolegniale-specific clades. Proteins of all clades, except one, contain an N-terminal microtubule interacting and trafficking (MIT) domain as predicted by protein domain databases or manual analysis, which is supported by homology modelling and comparison of conserved structural features from sequence logos. We identified at least three groups of CHSs conserved among all oomycete lineages and used phylogenetic reconciliation analysis to infer the dynamic evolution of CHSs in oomycetes. The evolutionary aspects of CHS diversity in modern-day oomycetes are discussed. In addition, we observed hyphal tip rupture in Phytophthora infestans upon treatment with the CHS inhibitor nikkomycin Z. Combining data on phylogeny, gene expression, and response to CHS inhibitors, we propose the association of different CHS clades with certain developmental stages. SN - 1095-9513 UR - https://www.unboundmedicine.com/medline/citation/31288106/Diversity_and_evolution_of_chitin_synthases_in_oomycetes__Straminipila:_Oomycota__ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1055-7903(18)30183-0 DB - PRIME DP - Unbound Medicine ER -