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Enzymes of early-diverging, zoosporic fungi
The secretome, the complement of extracellular proteins, is a reflection of the interaction of an organism with its host or substrate, thus a determining factor for the organism’s fitness and competitiveness. Hence, the secretome impacts speciation and organismal evolution. The zoosporic Chytridiomy...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6690862/ https://www.ncbi.nlm.nih.gov/pubmed/31309267 http://dx.doi.org/10.1007/s00253-019-09983-w |
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author | Lange, Lene Barrett, Kristian Pilgaard, Bo Gleason, Frank Tsang, Adrian |
author_facet | Lange, Lene Barrett, Kristian Pilgaard, Bo Gleason, Frank Tsang, Adrian |
author_sort | Lange, Lene |
collection | PubMed |
description | The secretome, the complement of extracellular proteins, is a reflection of the interaction of an organism with its host or substrate, thus a determining factor for the organism’s fitness and competitiveness. Hence, the secretome impacts speciation and organismal evolution. The zoosporic Chytridiomycota, Blastocladiomycota, Neocallimastigomycota, and Cryptomycota represent the earliest diverging lineages of the Fungal Kingdom. The review describes the enzyme compositions of these zoosporic fungi, underscoring the enzymes involved in biomass degradation. The review connects the lifestyle and substrate affinities of the zoosporic fungi to the secretome composition by examining both classical phenotypic investigations and molecular/genomic-based studies. The carbohydrate-active enzyme profiles of 19 genome-sequenced species are summarized. Emphasis is given to recent advances in understanding the functional role of rumen fungi, the basis for the devastating chytridiomycosis, and the structure of fungal cellulosome. The approach taken by the review enables comparison of the secretome enzyme composition of anaerobic versus aerobic early-diverging fungi and comparison of enzyme portfolio of specialized parasites, pathogens, and saprotrophs. Early-diverging fungi digest most major types of biopolymers: cellulose, hemicellulose, pectin, chitin, and keratin. It is thus to be expected that early-diverging fungi in its entirety represents a rich and diverse pool of secreted, metabolic enzymes. The review presents the methods used for enzyme discovery, the diversity of enzymes found, the status and outlook for recombinant production, and the potential for applications. Comparative studies on the composition of secretome enzymes of early-diverging fungi would contribute to unraveling the basal lineages of fungi. |
format | Online Article Text |
id | pubmed-6690862 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-66908622019-08-26 Enzymes of early-diverging, zoosporic fungi Lange, Lene Barrett, Kristian Pilgaard, Bo Gleason, Frank Tsang, Adrian Appl Microbiol Biotechnol Mini-Review The secretome, the complement of extracellular proteins, is a reflection of the interaction of an organism with its host or substrate, thus a determining factor for the organism’s fitness and competitiveness. Hence, the secretome impacts speciation and organismal evolution. The zoosporic Chytridiomycota, Blastocladiomycota, Neocallimastigomycota, and Cryptomycota represent the earliest diverging lineages of the Fungal Kingdom. The review describes the enzyme compositions of these zoosporic fungi, underscoring the enzymes involved in biomass degradation. The review connects the lifestyle and substrate affinities of the zoosporic fungi to the secretome composition by examining both classical phenotypic investigations and molecular/genomic-based studies. The carbohydrate-active enzyme profiles of 19 genome-sequenced species are summarized. Emphasis is given to recent advances in understanding the functional role of rumen fungi, the basis for the devastating chytridiomycosis, and the structure of fungal cellulosome. The approach taken by the review enables comparison of the secretome enzyme composition of anaerobic versus aerobic early-diverging fungi and comparison of enzyme portfolio of specialized parasites, pathogens, and saprotrophs. Early-diverging fungi digest most major types of biopolymers: cellulose, hemicellulose, pectin, chitin, and keratin. It is thus to be expected that early-diverging fungi in its entirety represents a rich and diverse pool of secreted, metabolic enzymes. The review presents the methods used for enzyme discovery, the diversity of enzymes found, the status and outlook for recombinant production, and the potential for applications. Comparative studies on the composition of secretome enzymes of early-diverging fungi would contribute to unraveling the basal lineages of fungi. Springer Berlin Heidelberg 2019-07-15 2019 /pmc/articles/PMC6690862/ /pubmed/31309267 http://dx.doi.org/10.1007/s00253-019-09983-w Text en © The Author(s) 2019 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Mini-Review Lange, Lene Barrett, Kristian Pilgaard, Bo Gleason, Frank Tsang, Adrian Enzymes of early-diverging, zoosporic fungi |
title | Enzymes of early-diverging, zoosporic fungi |
title_full | Enzymes of early-diverging, zoosporic fungi |
title_fullStr | Enzymes of early-diverging, zoosporic fungi |
title_full_unstemmed | Enzymes of early-diverging, zoosporic fungi |
title_short | Enzymes of early-diverging, zoosporic fungi |
title_sort | enzymes of early-diverging, zoosporic fungi |
topic | Mini-Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6690862/ https://www.ncbi.nlm.nih.gov/pubmed/31309267 http://dx.doi.org/10.1007/s00253-019-09983-w |
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