Comparative Molecular Evolution of Trichoderma Chitinases in Response to Mycoparasitic Interactions
(2010) In Evolutionary Bioinformatics 6. p.1-25- Abstract
- Certain species of the fungal genus Trichoderma are potent mycoparasites and are used for biological control of fungal diseases on agricultural crops. In Trichoderma, whole-genome sequencing reveal between 20 and 36 different genes encoding chitinases, hydrolytic enzymes that are involved in the mycoparasitic attack. Sequences of Trichoderma chitinase genes chi18-5, chi18-13, chi18-15 and chi18-17, which all exhibit specific expression during mycoparasitism-related conditions, were determined from up to 13 different taxa and studied with regard to their evolutionary patterns. Two of them, chi18-13 and chi18-17, are members of the B1/B2 chitinase subgroup that have expanded significantly in paralog number in mycoparasitic Hypocrea... (More)
- Certain species of the fungal genus Trichoderma are potent mycoparasites and are used for biological control of fungal diseases on agricultural crops. In Trichoderma, whole-genome sequencing reveal between 20 and 36 different genes encoding chitinases, hydrolytic enzymes that are involved in the mycoparasitic attack. Sequences of Trichoderma chitinase genes chi18-5, chi18-13, chi18-15 and chi18-17, which all exhibit specific expression during mycoparasitism-related conditions, were determined from up to 13 different taxa and studied with regard to their evolutionary patterns. Two of them, chi18-13 and chi18-17, are members of the B1/B2 chitinase subgroup that have expanded significantly in paralog number in mycoparasitic Hypocrea atroviridis and H. virens. Chi18-13 contains two codons that evolve under positive selection and seven groups of co-evolving sites. Chi18-15 displays a unique codon-usage and contains five codons that evolve under positive selection and three groups of co-evolving sites. Regions of high amino acid variability are preferentially localized to substrate-or product side of the catalytic clefts. Differences in amino acid diversity/conservation patterns between different Trichoderma clades are observed. These observations show that Trichoderma chitinases chi18-13 and chi18-15 evolve in a manner consistent with rapid co-evolutionary interactions and identifies putative target regions involved in determining substrate-specificity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1588428
- author
- Ihrmark, Katarina ; Asmail, Nashwan ; Ubhayasekera, Wimal LU ; Melin, Petter ; Stenlid, Jan and Karlsson, Magnus
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- chitinase, mycoparasitism, protein evolution, Trichoderma
- in
- Evolutionary Bioinformatics
- volume
- 6
- pages
- 1 - 25
- publisher
- Libertas Academica
- external identifiers
-
- wos:000275600100001
- scopus:77951266103
- ISSN
- 1176-9343
- language
- English
- LU publication?
- yes
- id
- d56fed6c-21fd-448f-a428-3cb4366dceec (old id 1588428)
- alternative location
- http://www.la-press.com/comparative-molecular-evolution-of-trichoderma-chitinases-in-response--a1919
- date added to LUP
- 2016-04-01 13:45:06
- date last changed
- 2022-01-27 20:53:52
@article{d56fed6c-21fd-448f-a428-3cb4366dceec, abstract = {{Certain species of the fungal genus Trichoderma are potent mycoparasites and are used for biological control of fungal diseases on agricultural crops. In Trichoderma, whole-genome sequencing reveal between 20 and 36 different genes encoding chitinases, hydrolytic enzymes that are involved in the mycoparasitic attack. Sequences of Trichoderma chitinase genes chi18-5, chi18-13, chi18-15 and chi18-17, which all exhibit specific expression during mycoparasitism-related conditions, were determined from up to 13 different taxa and studied with regard to their evolutionary patterns. Two of them, chi18-13 and chi18-17, are members of the B1/B2 chitinase subgroup that have expanded significantly in paralog number in mycoparasitic Hypocrea atroviridis and H. virens. Chi18-13 contains two codons that evolve under positive selection and seven groups of co-evolving sites. Chi18-15 displays a unique codon-usage and contains five codons that evolve under positive selection and three groups of co-evolving sites. Regions of high amino acid variability are preferentially localized to substrate-or product side of the catalytic clefts. Differences in amino acid diversity/conservation patterns between different Trichoderma clades are observed. These observations show that Trichoderma chitinases chi18-13 and chi18-15 evolve in a manner consistent with rapid co-evolutionary interactions and identifies putative target regions involved in determining substrate-specificity.}}, author = {{Ihrmark, Katarina and Asmail, Nashwan and Ubhayasekera, Wimal and Melin, Petter and Stenlid, Jan and Karlsson, Magnus}}, issn = {{1176-9343}}, keywords = {{chitinase; mycoparasitism; protein evolution; Trichoderma}}, language = {{eng}}, pages = {{1--25}}, publisher = {{Libertas Academica}}, series = {{Evolutionary Bioinformatics}}, title = {{Comparative Molecular Evolution of Trichoderma Chitinases in Response to Mycoparasitic Interactions}}, url = {{http://www.la-press.com/comparative-molecular-evolution-of-trichoderma-chitinases-in-response--a1919}}, volume = {{6}}, year = {{2010}}, }