A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases
- 8 November 2005
- journal article
- research article
- Published by Wiley in The FEBS Journal
- Vol. 272 (22) , 5923-5939
- https://doi.org/10.1111/j.1742-4658.2005.04994.x
Abstract
Genome‐wide analysis of chitinase genes in the Hypocrea jecorina (anamorph: Trichoderma reesei) genome database revealed the presence of 18 ORFs encoding putative chitinases, all of them belonging to glycoside hydrolase family 18. Eleven of these encode yet undescribed chitinases. A systematic nomenclature for the H. jecorina chitinases is proposed, which designates the chitinases corresponding to their glycoside hydrolase family and numbers the isoenzymes according to their pI from Chi18‐1 to Chi18‐18. Phylogenetic analysis of H. jecorina chitinases, and those from other filamentous fungi, including hypothetical proteins of annotated fungal genome databases, showed that the fungal chitinases can be divided into three groups: groups A and B (corresponding to class V and III chitinases, respectively) also contained the so Trichoderma chitinases identified to date, whereas a novel group C comprises high molecular weight chitinases that have a domain structure similar to Kluyveromyces lactis killer toxins. Five chitinase genes, representing members of groups A–C, were cloned from the mycoparasitic species H. atroviridis (anamorph: T. atroviride). Transcription of chi18‐10 (belonging to group C) and chi18‐13 (belonging to a novel clade in group B) was triggered upon growth on Rhizoctonia solani cell walls, and during plate confrontation tests with the plant pathogen R. solani. Therefore, group C and the novel clade in group B may contain chitinases of potential relevance for the biocontrol properties of Trichoderma.Keywords
This publication has 82 references indexed in Scilit:
- Phylogeny and evolution of the genus Trichoderma: a multigene approachMycological Research, 2002
- Predicting Subcellular Localization of Proteins Based on their N-terminal Amino Acid SequenceJournal of Molecular Biology, 2000
- The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD) 1 1Edited by P. E. WightJournal of Molecular Biology, 2000
- The 1.8 Å Resolution Structure of Hevamine, a Plant Chitinase/Lysozyme, and Analysis of the Conserved Sequence and Structure Motifs of Glycosyl Hydrolase Family 18Journal of Molecular Biology, 1996
- Crel, the carbon catabolite repressor protein from Trichoderma reeseiFEBS Letters, 1995
- The refined crystal structure of an endochitinasefrom Hordeum vulgare L. seeds at 1.8 Å resolutionJournal of Molecular Biology, 1995
- Isolation and sequence of an endochitinase-encoding gene from a cDNA library of Trichoderma harzianumGene, 1994
- Isolation of Trichoderma reesei genes highly expressed on glucose-containing media: characterization of the tef1 gene encoding translation elongation factor 1αGene, 1993
- Evolution of a family ofN-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutininJournal of Molecular Evolution, 1991
- Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealingBiochemistry, 1989