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Article: A stilbene synthase gene (SbSTS1) is involved in host and nonhost defense responses in sorghum

TitleA stilbene synthase gene (SbSTS1) is involved in host and nonhost defense responses in sorghum
Authors
Issue Date2005
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 2005, v. 138 n. 1, p. 393-401 How to Cite?
AbstractA chalcone synthase (CHS)-like gene, SbCHS8, with high expressed sequence tag abundance in a pathogen-induced cDNA library, was identified previously in sorghum (Sorghum bicolor). Genomic Southern analysis revealed that SbCHS8 represents a single-copy gene. SbCHS8 expression was induced in sorghum mesocotyls following inoculation with Cochliobolus heterotrophus and Colletotrichum sublineolum, corresponding to nonhost and host defense responses, respectively. However, the induction was delayed by approximately 24 h when compared to the expression of at least one of the other SbCHS genes. In addition, SbCHS8 expression was not induced by light and did not occur in a tissue-specific manner. SbCHS8, together with SbCHS2, was overexpressed in transgenic Arabidopsis (Arabidopsis thaliana) tt4 (transparent testa) mutants defective in CHS activities. SbCHS2 rescued the ability of these mutants to accumulate flavonoids in seed coats and seedlings. In contrast, SbCHS8 failed to complement the mutation, suggesting that the encoded enzyme does not function as a CHS. To elucidate their biochemical functions, recombinant proteins were assayed with different phenylpropanoid-Coenzyme A esters. Flavanones and stilbenes were detected in the reaction products of SbCHS2 and SbCHS8, respectively. Taken together, our data demonstrated that SbCHS2 encodes a typical CHS that synthesizes naringenin chalcone, which is necessary for the formation of different flavonoid metabolites. On the other hand, SbCHS8, now retermed SbSTS1, encodes an enzyme with stilbene synthase activity, suggesting that sorghum accumulates stilbene-derived defense metabolites in addition to the well-characterized 3-deoxyanthocyanidin phytoalexins. © 2005 American Society of Plant Biologists.
Persistent Identifierhttp://hdl.handle.net/10722/48509
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYu, CKYen_HK
dc.contributor.authorSpringob, Ken_HK
dc.contributor.authorSchmidt, Jen_HK
dc.contributor.authorNicholson, RLen_HK
dc.contributor.authorChu, IKen_HK
dc.contributor.authorWing, KYen_HK
dc.contributor.authorLo, Cen_HK
dc.date.accessioned2008-05-22T04:15:45Z-
dc.date.available2008-05-22T04:15:45Z-
dc.date.issued2005en_HK
dc.identifier.citationPlant Physiology, 2005, v. 138 n. 1, p. 393-401en_HK
dc.identifier.issn0032-0889en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48509-
dc.description.abstractA chalcone synthase (CHS)-like gene, SbCHS8, with high expressed sequence tag abundance in a pathogen-induced cDNA library, was identified previously in sorghum (Sorghum bicolor). Genomic Southern analysis revealed that SbCHS8 represents a single-copy gene. SbCHS8 expression was induced in sorghum mesocotyls following inoculation with Cochliobolus heterotrophus and Colletotrichum sublineolum, corresponding to nonhost and host defense responses, respectively. However, the induction was delayed by approximately 24 h when compared to the expression of at least one of the other SbCHS genes. In addition, SbCHS8 expression was not induced by light and did not occur in a tissue-specific manner. SbCHS8, together with SbCHS2, was overexpressed in transgenic Arabidopsis (Arabidopsis thaliana) tt4 (transparent testa) mutants defective in CHS activities. SbCHS2 rescued the ability of these mutants to accumulate flavonoids in seed coats and seedlings. In contrast, SbCHS8 failed to complement the mutation, suggesting that the encoded enzyme does not function as a CHS. To elucidate their biochemical functions, recombinant proteins were assayed with different phenylpropanoid-Coenzyme A esters. Flavanones and stilbenes were detected in the reaction products of SbCHS2 and SbCHS8, respectively. Taken together, our data demonstrated that SbCHS2 encodes a typical CHS that synthesizes naringenin chalcone, which is necessary for the formation of different flavonoid metabolites. On the other hand, SbCHS8, now retermed SbSTS1, encodes an enzyme with stilbene synthase activity, suggesting that sorghum accumulates stilbene-derived defense metabolites in addition to the well-characterized 3-deoxyanthocyanidin phytoalexins. © 2005 American Society of Plant Biologists.en_HK
dc.format.extent6690449 bytes-
dc.format.extent235804 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypeapplication/pdf-
dc.languageengen_HK
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.orgen_HK
dc.relation.ispartofPlant Physiologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshAcyltransferases - geneticsen_HK
dc.subject.meshGene Expression Regulation, Planten_HK
dc.subject.meshSorghum - enzymology - genetics - growth & development - microbiologyen_HK
dc.subject.meshAscomycota - pathogenicityen_HK
dc.subject.meshBase Sequenceen_HK
dc.titleA stilbene synthase gene (SbSTS1) is involved in host and nonhost defense responses in sorghumen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0032-0889&volume=138&issue=1&spage=393&epage=401&date=2005&atitle=A+stilbene+synthase+gene+(SbSTS1)+is+involved+in+host+and+nonhost+defense+responses+in+sorghumen_HK
dc.identifier.emailChu, IK: ivankchu@hku.hken_HK
dc.identifier.emailWing, KY: wkyip@hkucc.hku.hken_HK
dc.identifier.emailLo, C: clivelo@hkucc.hku.hken_HK
dc.identifier.authorityChu, IK=rp00683en_HK
dc.identifier.authorityWing, KY=rp00833en_HK
dc.identifier.authorityLo, C=rp00751en_HK
dc.description.naturepreprinten_HK
dc.identifier.doi10.1104/pp.105.059337en_HK
dc.identifier.pmid15821144-
dc.identifier.pmcidPMC1104192en_HK
dc.identifier.scopuseid_2-s2.0-27244440022en_HK
dc.identifier.hkuros98451-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-27244440022&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume138en_HK
dc.identifier.issue1en_HK
dc.identifier.spage393en_HK
dc.identifier.epage401en_HK
dc.identifier.isiWOS:000229023100038-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridYu, CKY=8932539000en_HK
dc.identifier.scopusauthoridSpringob, K=6507736131en_HK
dc.identifier.scopusauthoridSchmidt, J=35557450400en_HK
dc.identifier.scopusauthoridNicholson, RL=7201624684en_HK
dc.identifier.scopusauthoridChu, IK=7103327484en_HK
dc.identifier.scopusauthoridWing, KY=7102784428en_HK
dc.identifier.scopusauthoridLo, C=15737175700en_HK

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