2015
DOI: 10.1007/s00294-014-0471-9
|View full text |Cite
|
Sign up to set email alerts
|

Molecular diversity of LysM carbohydrate-binding motifs in fungi

Abstract: LysM motifs are carbohydrate-binding modules found in prokaryotes and eukaryotes. They bind to N-acetylglucosamine-containing carbohydrates, such as chitin, chitio-oligosaccharides and peptidoglycan. In this review, we summarize the features of the protein architecture of LysM-containing proteins in fungi and discuss their so far known biochemical properties, transcriptional profiles and biological functions. Further, based on data from evolutionary analyses and consensus pattern profiling of fungal LysM motif… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

4
89
0
3

Year Published

2016
2016
2024
2024

Publication Types

Select...
6
2
1

Relationship

0
9

Authors

Journals

citations
Cited by 91 publications
(96 citation statements)
references
References 52 publications
4
89
0
3
Order By: Relevance
“…1a, Supplementary Table 5). In other plant pathogens, these are involved in modifying fungal cell wall composition and/or capturing chitin residues to mask chitin-triggered immune signals and evade detection by the host plants [21][22][23][24][25] , suggesting similar roles in Armillaria.…”
Section: Resultsmentioning
confidence: 99%
“…1a, Supplementary Table 5). In other plant pathogens, these are involved in modifying fungal cell wall composition and/or capturing chitin residues to mask chitin-triggered immune signals and evade detection by the host plants [21][22][23][24][25] , suggesting similar roles in Armillaria.…”
Section: Resultsmentioning
confidence: 99%
“…We identified other putative chitin-related proteins that have carbohydrate-binding module family 50 domains (CBM50, known as the LysM domain). Several LysM domains have chitin-binding ability, and several chitinases contain LysM domains (50). We found 7 proteins containing CMB50 domains; 5 of 7 such proteins were increased after harvest, and 2 of 5 were identified as DEGs in the fruiting body after harvest (g6653.t1 and g8231.t1) ( Table 4).…”
Section: Resultsmentioning
confidence: 87%
“…6%). Among these the LysM motif (CBM50) has attracted most attention [56]. This module has general N-acetylglucosamine binding properties and is therefore able to bind to chitin or chitin-like carbohydrates [57].…”
Section: Resultsmentioning
confidence: 99%