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Article: Tobacco-expressed Brassica juncea chitinase BjCHI1 shows antifungal activity in vitro

TitleTobacco-expressed Brassica juncea chitinase BjCHI1 shows antifungal activity in vitro
Authors
KeywordsAspergillus infection
Caterpillar feeding
Chitin-binding domain
Fungal induction
PR protein
Tobacco transformation
Issue Date2002
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412
Citation
Plant Molecular Biology, 2002, v. 50 n. 2, p. 283-294 How to Cite?
AbstractWe have previously isolated a Brassica juncea cDNA encoding BjCHI1, a novel chitinase with two chitin-binding domains, and have shown that its mRNA is induced by wounding and methyl jasmonate treatment (K.-J. Zhao and M.-L. Chye, Plant Mol. Biol. 40 (1999) 1009-1018). By the presence of two chitin-binding domains, BjCHI1 resembles the precursor of UDA (Urtica dioica agglutinin) but, unlike UDA, BjCHI1 retains its chitinase catalytic domain after post-translational processing. Here, we indicate the role of BjCHI1 in plant defense by demonstrating its mRNA induction upon Aspergillus niger infection or caterpillar Pieris rapae (L.) feeding. To further investigate the biological properties of BjCHI1, we transformed tobacco with a construct expressing the BjCHI1 cDNA from the CaMV 35S promoter. Subsequently, we purified BjCHI1 from the resultant transgenic R0 plants using a regenerated chitin column followed by fast protein liquid chromatography (FPLC). Also, the significance of the second chitin-binding domain in BjCHI1 was investigated by raising transgenic tobacco plants expressing BJCHI2, a deletion derivative of BjCHI1 lacking one chitin-binding domain. Colorimetric chitinase assays at 25°C, pH 5, showed no significant differences between the activities of BjCHI1 and BJCHI2, suggesting that chitinase activity, due to the catalytic domain, is not enhanced by the presence of a second chitin-binding domain. Both BjCHI1 and BJCHI2 show in vitro anti-fungal activity toward Trichoderma viride, causing reductions in hyphal diameter, hyphal branching and conidia size.
Persistent Identifierhttp://hdl.handle.net/10722/68531
ISSN
2015 Impact Factor: 3.905
2015 SCImago Journal Rankings: 1.915
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFung, KLen_HK
dc.contributor.authorZhao, KJen_HK
dc.contributor.authorHe, ZMen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2010-09-06T06:05:26Z-
dc.date.available2010-09-06T06:05:26Z-
dc.date.issued2002en_HK
dc.identifier.citationPlant Molecular Biology, 2002, v. 50 n. 2, p. 283-294en_HK
dc.identifier.issn0167-4412en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68531-
dc.description.abstractWe have previously isolated a Brassica juncea cDNA encoding BjCHI1, a novel chitinase with two chitin-binding domains, and have shown that its mRNA is induced by wounding and methyl jasmonate treatment (K.-J. Zhao and M.-L. Chye, Plant Mol. Biol. 40 (1999) 1009-1018). By the presence of two chitin-binding domains, BjCHI1 resembles the precursor of UDA (Urtica dioica agglutinin) but, unlike UDA, BjCHI1 retains its chitinase catalytic domain after post-translational processing. Here, we indicate the role of BjCHI1 in plant defense by demonstrating its mRNA induction upon Aspergillus niger infection or caterpillar Pieris rapae (L.) feeding. To further investigate the biological properties of BjCHI1, we transformed tobacco with a construct expressing the BjCHI1 cDNA from the CaMV 35S promoter. Subsequently, we purified BjCHI1 from the resultant transgenic R0 plants using a regenerated chitin column followed by fast protein liquid chromatography (FPLC). Also, the significance of the second chitin-binding domain in BjCHI1 was investigated by raising transgenic tobacco plants expressing BJCHI2, a deletion derivative of BjCHI1 lacking one chitin-binding domain. Colorimetric chitinase assays at 25°C, pH 5, showed no significant differences between the activities of BjCHI1 and BJCHI2, suggesting that chitinase activity, due to the catalytic domain, is not enhanced by the presence of a second chitin-binding domain. Both BjCHI1 and BJCHI2 show in vitro anti-fungal activity toward Trichoderma viride, causing reductions in hyphal diameter, hyphal branching and conidia size.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412en_HK
dc.relation.ispartofPlant Molecular Biologyen_HK
dc.subjectAspergillus infectionen_HK
dc.subjectCaterpillar feedingen_HK
dc.subjectChitin-binding domainen_HK
dc.subjectFungal inductionen_HK
dc.subjectPR proteinen_HK
dc.subjectTobacco transformationen_HK
dc.titleTobacco-expressed Brassica juncea chitinase BjCHI1 shows antifungal activity in vitroen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0167-4412&volume=50&spage=283&epage=294&date=2002&atitle=Tobacco-expressed+Brassica+juncea+chitinase+BjCHI1+shows+antifungal+activity+in+vitroen_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1023/A:1016067200148en_HK
dc.identifier.pmid12175020-
dc.identifier.scopuseid_2-s2.0-0036717162en_HK
dc.identifier.hkuros75785en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036717162&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume50en_HK
dc.identifier.issue2en_HK
dc.identifier.spage283en_HK
dc.identifier.epage294en_HK
dc.identifier.isiWOS:000176462800012-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridFung, KL=7202935039en_HK
dc.identifier.scopusauthoridZhao, KJ=7202071954en_HK
dc.identifier.scopusauthoridHe, ZM=15059027100en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK

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