English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Cellulose degradation in Gastrophysa viridula (Coleoptera: Chrysomelidae): functional characterization of two CAZymes belonging to glycoside hydrolase family 45 reveals a novel enzymatic activity

Busch, A., Kunert, G., Wielsch, N., & Pauchet, Y. (2018). Cellulose degradation in Gastrophysa viridula (Coleoptera: Chrysomelidae): functional characterization of two CAZymes belonging to glycoside hydrolase family 45 reveals a novel enzymatic activity. Insect Molecular Biology, 27(5), 633-650. doi:10.1111/imb.12500.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
HEC393s1.zip (Supplementary material), 14MB
 
File Permalink:
-
Name:
HEC393s1.zip
Description:
-
Visibility:
Restricted (Max Planck Institute for Chemical Ecology, MJCO; )
MIME-Type / Checksum:
application/zip
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
HEC393.pdf (Publisher version), 528KB
 
File Permalink:
-
Name:
HEC393.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Chemical Ecology, MJCO; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Busch, André1, 2, Author              
Kunert, Grit3, Author              
Wielsch, Natalie4, Author              
Pauchet, Yannick1, Author              
Affiliations:
1Department of Entomology, Prof. D. G. Heckel, MPI for Chemical Ecology, Max Planck Society, ou_421895              
2IMPRS on Ecological Interactions, MPI for Chemical Ecology, Max Planck Society, Jena, DE, ou_421900              
3Statistical Service, Dr. Grit Kunert, MPI for Chemical Ecology, Max Planck Society, ou_3171479              
4Research Group Mass Spectrometry, MPI for Chemical Ecology, Max Planck Society, ou_421899              

Content

show
hide
Free keywords: -
 Abstract: Cellulose is a major component of the primary and secondary cell walls in plants. Cellulose is considered to be the most abundant biopolymer on Earth and represents a large potential source of metabolic energy. Yet, cellulose degradation is rare and mostly restricted to cellulolytic microorganisms. Recently, various metazoans, including leaf beetles, have been found to encode their own cellulases, giving them the ability to degrade cellulose independently of cellulolytic symbionts. Here, we analyzed the cellulosic capacity of the leaf beetle Gastrophysa viridula, which typically feeds on Rumex plants. We identified three putative cellulases member of two glycoside hydrolase (GH) families, namely GH45 and GH9. Using heterologous expression and functional assays, we demonstrated that both GH45 proteins are active enzymes, in contrast to the GH9 protein. One GH45 protein acted on amorphous cellulose as an endo-β-1,4-glucanase, whereas the other evolved to become an endo-β-1,4-xyloglucanase. We successfully knocked down the expression of both GH45 genes using RNAi, but no changes in weight gain or mortality were observed compared to control insects. Our data indicated that the breakdown of these polysaccharides in G. viridula may facilitate access to plant cell content, which is rich in nitrogen and simple sugars.

Details

show
hide
Language(s):
 Dates: 2018-052018-05-172018-09
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: HEC393
DOI: 10.1111/imb.12500
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Insect Molecular Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Oxford : Published for the Royal Entomological Society by Blackwell Scientific Publications
Pages: - Volume / Issue: 27 (5) Sequence Number: - Start / End Page: 633 - 650 Identifier: ISSN: 0962-1075
CoNE: https://pure.mpg.de/cone/journals/resource/954925580118