ArticleBMC microbiology2018
Evolution and functional characterization of pectate lyase PEL12, a member of a highly expanded Clonostachys rosea polysaccharide lyase 1 family.
Article in BMC microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 43 citations in OpenAlex.
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- Molecular Characterization of a Novel Alkaline Endo-Pectate Lyase fromMolecules (Basel, Switzerland) · 2025Article
- Temporal proteome profiling of Botrytis cinerea reveals proteins involved in plant invasion and survival.Scientific reports · 2025Article
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- Improvement on Thermostability of Pectate Lyase and Its Potential Application to Ramie Degumming.Polymers · 2022Article
- Discovery of a Novel Glucuronan Lyase System inApplied and environmental microbiology · 2022Article
- A Comprehensive Insight into Fungal Enzymes: Structure, Classification, and Their Role in Mankind's Challenges.Journal of fungi (Basel, Switzerland) · 2021Review
- Genetic determinants of endophytism in the Arabidopsis root mycobiome.Nature communications · 2021Article
- Comparative analysis of draft genome assemblies developed from whole genome sequences of twoBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- Comparative genome analyses suggest a hemibiotrophic lifestyle and virulence differences for the beech bark disease fungal pathogens Neonectria faginata and Neonectria coccinea.G3 (Bethesda, Md.) · 2021Article
- Comparative genomics highlights the importance of drug efflux transporters during evolution of mycoparasitism inEvolutionary applications · 2021Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPectin is one of the major and most complex plant cell wall components that needs to be overcome by microorganisms as part of their strategies for plant invasion or nutrition. Microbial pectinolytic enzymes therefore play a significant role for plant-associated microorganisms and for the decomposition and recycling of plant organic matter. Recently, comparative studies revealed significant gene copy number expansion of the polysaccharide lyase 1 (PL1) pectin/pectate lyase gene family in the Clonostachys rosea genome, while only low numbers were found in Trichoderma species. Both of these fungal genera are widely known for their ability to parasitize and kill other fungi (mycoparasitism) and certain species are thus used for biocontrol of plant pathogenic fungi.
resultsIn order to understand the role of the high number of pectin degrading enzymes in Clonostachys, we studied diversity and evolution of the PL1 gene family in C. rosea compared with other Sordariomycetes with varying nutritional life styles. Out of 17 members of C. rosea PL1, we could only detect two to be secreted at acidic pH. One of them, the pectate lyase pel12 gene was found to be strongly induced by pectin and, to a lower degree, by polygalacturonic acid. Heterologous expression of the PEL12 in a PL1-free background of T. reesei revealed direct enzymatic involvement of this protein in utilization of pectin at pH 5 without a requirement for Ca
conclusionsIn this study, we aimed to gain insight into diversity and evolution of the PL1 gene family in C. rosea and other Sordariomycete species in relation to their nutritional modes. We show that C. rosea PL1 expansion does not correlate with its mycoparasitic nutritional mode and resembles those of strong plant pathogenic fungi. We further investigated regulation, specificity and function of the C. rosea PEL12 and show that this enzyme is directly involved in degradation of pectin and pectin-related compounds, but not in C. rosea biocontrol.
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