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Conference Paper: Acyl-CoA-binding protein families in the plant kingdom

TitleAcyl-CoA-binding protein families in the plant kingdom
Authors
Issue Date2011
PublisherSociety for Experimental Biology.
Citation
The 2011 Annual Main Meeting of the Society for Experimental Biolog (SEB), Glasgow, U.K., 1-4 July 2011. In Abstract Book of the SEB Annual Main Meeting, 2011, p. 223 How to Cite?
AbstractAcyl-CoA-binding proteins (ACBPs), ubiquitous in eukaryotes, participate in lipid metabolism by binding acyl-CoA esters at the conserved acyl-CoA-binding (ACB) domain. Phylogenetic analyses on 16 plant genomes comprising green alga, mosses, gymnosperm, monocots and dicots revealed that the ACBP family expanded with the evolution of land plants. The plant ACBP family is clustered into four groups, designated as Class I to Class IV. Class I is identical to the prototype ACBP protein (10-kDa) that has been well-studied in mammals and yeast. Class II and Class IV proteins consist of an ACB domain as well as ankyrin repeats or kelch motifs, respectively. Class III proteins form larger proteins that contain an ACB domain. Classes I and IV seemed to have evolved independently, while Classes II and III are closely related phylogenetically. The ACBP family in the eudicot model plant, Arabidopsis, has six members that have been previously characterized. The ACBP family in the monocot, rice, also consists of six members but their distribution across the four classes differ from Arabidopsis. There are three Class I members in rice, while only one occurs in Arabidopsis. Furthermore, two each of Class II and Class IV have been identified in Arabidopsis while one each exists in rice. However, only one Class III member is present in both Arabidopsis and rice. Results from our investigations suggest that rice ACBPs have non-overlapping functions and the larger and multi-domain forms appear to be related to stress responses.
DescriptionPoster Session: P4 - Integration of abiotic and biotic stress responses: from systems biology to field: abstract P4.34
Persistent Identifierhttp://hdl.handle.net/10722/138283

 

DC FieldValueLanguage
dc.contributor.authorMeng, Wen_US
dc.contributor.authorSu, Yen_US
dc.contributor.authorSaunders, Ren_US
dc.contributor.authorChye, MLen_US
dc.date.accessioned2011-08-26T14:44:20Z-
dc.date.available2011-08-26T14:44:20Z-
dc.date.issued2011en_US
dc.identifier.citationThe 2011 Annual Main Meeting of the Society for Experimental Biolog (SEB), Glasgow, U.K., 1-4 July 2011. In Abstract Book of the SEB Annual Main Meeting, 2011, p. 223en_US
dc.identifier.urihttp://hdl.handle.net/10722/138283-
dc.descriptionPoster Session: P4 - Integration of abiotic and biotic stress responses: from systems biology to field: abstract P4.34-
dc.description.abstractAcyl-CoA-binding proteins (ACBPs), ubiquitous in eukaryotes, participate in lipid metabolism by binding acyl-CoA esters at the conserved acyl-CoA-binding (ACB) domain. Phylogenetic analyses on 16 plant genomes comprising green alga, mosses, gymnosperm, monocots and dicots revealed that the ACBP family expanded with the evolution of land plants. The plant ACBP family is clustered into four groups, designated as Class I to Class IV. Class I is identical to the prototype ACBP protein (10-kDa) that has been well-studied in mammals and yeast. Class II and Class IV proteins consist of an ACB domain as well as ankyrin repeats or kelch motifs, respectively. Class III proteins form larger proteins that contain an ACB domain. Classes I and IV seemed to have evolved independently, while Classes II and III are closely related phylogenetically. The ACBP family in the eudicot model plant, Arabidopsis, has six members that have been previously characterized. The ACBP family in the monocot, rice, also consists of six members but their distribution across the four classes differ from Arabidopsis. There are three Class I members in rice, while only one occurs in Arabidopsis. Furthermore, two each of Class II and Class IV have been identified in Arabidopsis while one each exists in rice. However, only one Class III member is present in both Arabidopsis and rice. Results from our investigations suggest that rice ACBPs have non-overlapping functions and the larger and multi-domain forms appear to be related to stress responses.-
dc.languageengen_US
dc.publisherSociety for Experimental Biology.-
dc.relation.ispartofSEB Glasgrow 2011en_US
dc.titleAcyl-CoA-binding protein families in the plant kingdomen_US
dc.typeConference_Paperen_US
dc.identifier.emailMeng, W: mengwei@hku.hken_US
dc.identifier.emailSu, Y: ycfsu@hkucc.hku.hken_US
dc.identifier.emailSaunders, R: saunders@hkucc.hku.hken_US
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hk-
dc.identifier.authoritySaunders, R=rp00774en_US
dc.identifier.authorityChye, ML=rp00687en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.hkuros189831en_US
dc.identifier.spage223en_US
dc.identifier.epage223en_US
dc.publisher.placeUnited Kingdom-
dc.description.otherThe 2011 Annual Main Meeting of the Society for Experimental Biolog (SEB), Glasgow, U.K., 1-4 July 2011. In Abstract Book of the SEB Annual Main Meeting, 2011, p. 223-

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