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Article: The rice acyl-CoA-binding protein gene family: Phylogeny, expression and functional analysis

TitleThe rice acyl-CoA-binding protein gene family: Phylogeny, expression and functional analysis
Authors
KeywordsAcyl-CoA esters
Acyl-CoA-binding protein (ACBP)
Evolution
Expression profiles
Monocot
Oryza sativa
Issue Date2011
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPH
Citation
New Phytologist, 2011, v. 189 n. 4, p. 1170-1184 How to Cite?
AbstractAcyl-CoA-binding proteins (ACBPs) show conservation in an acyl-CoA-binding domain (ACB domain) which binds acyl-CoA esters. Previous studies on plant ACBPs focused on eudicots, Arabidopsis and Brassica. Here, we report on the phylogeny and characterization of the ACBP family from the monocot Oryza sativa (rice). Phylogenetic analyses were conducted using 16 plant genomes. Expression profiles of rice ACBPs under normal growth, as well as biotic and abiotic stress conditions, were examined by quantitative real-time reverse-transcription polymerase chain reactions. In vitro acyl-CoA-binding assays were conducted using recombinant (His)6-tagged ACBPs. The ACBP family diversified as land plants evolved. Classes I and IV show lineage-specific gene expansion. Classes II and III are closely related phylogenetically. As in the eudicot Arabidopsis, six genes (designated OsACBP1 to OsACBP6) encode rice ACBPs, but their distribution into various classes differed from Arabidopsis. Rice ACBP mRNAs showed ubiquitous expression and OsACBP4, OsACBP5 and OsACBP6 were stress-responsive. All recombinant rice ACBPs bind [14C]linolenoyl-CoA besides having specific substrates. Phylogeny, gene expression and biochemical analyses suggest that paralogues within and across classes are not redundant proteins. In addition to performing conserved basal functions, multidomain rice ACBPs appear to be associated with stress responses. © 2010 The Authors. New Phytologist © 2010 New Phytologist Trust.
Persistent Identifierhttp://hdl.handle.net/10722/142967
ISSN
2015 Impact Factor: 7.21
2015 SCImago Journal Rankings: 3.603
ISI Accession Number ID
Funding AgencyGrant Number
University of Hong Kong10400274
Funding Information:

We thank C. Lo and W. K. Yip (The University of Hong Kong) for provision of rice (O. sativa cv Zhonghua 11) seeds and the LS 6500 liquid scintillation counter, respectively. H. M. Lam (The Chinese University of Hong Kong) kindly provided us with rice blast fungus. We also thank S. Xiao for suggestions and discussion on the manuscript. This work was supported by the University of Hong Kong (CRCG Grant 10400274 and postgraduate studentship awarded to WM).

References

 

DC FieldValueLanguage
dc.contributor.authorMeng, Wen_HK
dc.contributor.authorSu, YCFen_HK
dc.contributor.authorSaunders, RMKen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2011-10-28T03:00:20Z-
dc.date.available2011-10-28T03:00:20Z-
dc.date.issued2011en_HK
dc.identifier.citationNew Phytologist, 2011, v. 189 n. 4, p. 1170-1184en_HK
dc.identifier.issn0028-646Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/142967-
dc.description.abstractAcyl-CoA-binding proteins (ACBPs) show conservation in an acyl-CoA-binding domain (ACB domain) which binds acyl-CoA esters. Previous studies on plant ACBPs focused on eudicots, Arabidopsis and Brassica. Here, we report on the phylogeny and characterization of the ACBP family from the monocot Oryza sativa (rice). Phylogenetic analyses were conducted using 16 plant genomes. Expression profiles of rice ACBPs under normal growth, as well as biotic and abiotic stress conditions, were examined by quantitative real-time reverse-transcription polymerase chain reactions. In vitro acyl-CoA-binding assays were conducted using recombinant (His)6-tagged ACBPs. The ACBP family diversified as land plants evolved. Classes I and IV show lineage-specific gene expansion. Classes II and III are closely related phylogenetically. As in the eudicot Arabidopsis, six genes (designated OsACBP1 to OsACBP6) encode rice ACBPs, but their distribution into various classes differed from Arabidopsis. Rice ACBP mRNAs showed ubiquitous expression and OsACBP4, OsACBP5 and OsACBP6 were stress-responsive. All recombinant rice ACBPs bind [14C]linolenoyl-CoA besides having specific substrates. Phylogeny, gene expression and biochemical analyses suggest that paralogues within and across classes are not redundant proteins. In addition to performing conserved basal functions, multidomain rice ACBPs appear to be associated with stress responses. © 2010 The Authors. New Phytologist © 2010 New Phytologist Trust.en_HK
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPHen_HK
dc.relation.ispartofNew Phytologisten_HK
dc.rightsThe definitive version is available at www.blackwell-synergy.com-
dc.subjectAcyl-CoA estersen_HK
dc.subjectAcyl-CoA-binding protein (ACBP)en_HK
dc.subjectEvolutionen_HK
dc.subjectExpression profilesen_HK
dc.subjectMonocoten_HK
dc.subjectOryza sativaen_HK
dc.titleThe rice acyl-CoA-binding protein gene family: Phylogeny, expression and functional analysisen_HK
dc.typeArticleen_HK
dc.identifier.emailSaunders, RMK: saunders@hkucc.hku.hken_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authoritySaunders, RMK=rp00774en_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1111/j.1469-8137.2010.03546.xen_HK
dc.identifier.pmid21128943-
dc.identifier.scopuseid_2-s2.0-79551553402en_HK
dc.identifier.hkuros184557en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79551553402&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume189en_HK
dc.identifier.issue4en_HK
dc.identifier.spage1170en_HK
dc.identifier.epage1184en_HK
dc.identifier.eissn1469-8137-
dc.identifier.isiWOS:000286940500027-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridMeng, W=36918822200en_HK
dc.identifier.scopusauthoridSu, YCF=7404456219en_HK
dc.identifier.scopusauthoridSaunders, RMK=35345489600en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK
dc.identifier.citeulike8401631-

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