Potato Resistance Against Insect Herbivores

Pelletier, Y; Horgan, FG; Pompon, J

Potato Resistance Against Insect Herbivores

Pelletier, Y Horgan, FG

Pompon, J

Permalink

Publisher:: Global Science Books
Publication Type:: Journal Article
Citation:: The Americas Journal of Plant Science and Biotechnology, 2011, 5 (S1), pp. 37 - 52
Issue Date:: 2011

Open Access

Copyright Clearance Process

Recently Added
In Progress
Open Access

This item is open access.

Adobe PDF

Download Published VersionAdobe PDF (294.82 kB)

View statistics

Full metadata record

Field	Value	Language
dc.contributor.author	Pelletier, Y	en_US
dc.contributor.author	Horgan, FG https://orcid.org/0000-0003-3796-667X	en_US
dc.contributor.author	Pompon, J	en_US
dc.date.issued	2011	en_US
dc.identifier.citation	The Americas Journal of Plant Science and Biotechnology, 2011, 5 (S1), pp. 37 - 52	en_US
dc.identifier.issn	1752-3877	en_US
dc.identifier.uri	http://hdl.handle.net/10453/119529
dc.description.abstract	Invited Review: Over the last two decades scientists have focused much attention on the physiological, molecular and functional biology of plant chitinases and there is considerable evidence suggest that chitinases play important roles in plant defense systems. Chitinases have also been shown to play a role in plant growth and development. Several review articles exist for chitinases of angiosperms but there is no such review for conifer chitinases, despite the economic and ecological significance of coniferous species in the world’s forests. Conifer chitinases consist of at least several classes of enzymes that are represented by small gene families. Class II (acidic) and class IV (basic) chitinases, expressed differentially over time and space, have been shown to be the major defense players in many conifer pathosystems. Class I and III chitinases are also reported in some conifers. This review discusses the current body of knowledge regarding conifer chitinases, including the molecular structure of chitinase genes and their regulation and function in conifer plants. Future potential uses for conifer chitinases as biopesticides	en_US
dc.publisher	Global Science Books	en_US
dc.relation.ispartof	The Americas Journal of Plant Science and Biotechnology	en_US
dc.title	Potato Resistance Against Insect Herbivores	en_US
dc.type	Journal Article
utslib.citation.volume	S1	en_US
utslib.citation.volume	5	en_US
utslib.for	0703 Crop and Pasture Production	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	open_access
pubs.consider-herdc	false	en_US
pubs.issue	S1	en_US
pubs.publication-status	Published	en_US
pubs.volume	5	en_US

Abstract:

Invited Review: Over the last two decades scientists have focused much attention on the physiological, molecular and functional biology of plant chitinases and there is considerable evidence suggest that chitinases play important roles in plant defense systems. Chitinases have also been shown to play a role in plant growth and development. Several review articles exist for chitinases of angiosperms but there is no such review for conifer chitinases, despite the economic and ecological significance of coniferous species in the world’s forests. Conifer chitinases consist of at least several classes of enzymes that are represented by small gene families. Class II (acidic) and class IV (basic) chitinases, expressed differentially over time and space, have been shown to be the major defense players in many conifer pathosystems. Class I and III chitinases are also reported in some conifers. This review discusses the current body of knowledge regarding conifer chitinases, including the molecular structure of chitinase genes and their regulation and function in conifer plants. Future potential uses for conifer chitinases as biopesticides

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/119529