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Article: A dual-targeted purple acid phosphatase in Arabidopsis thaliana moderates carbon metabolism and its overexpression leads to faster plant growth and higher seed yield

TitleA dual-targeted purple acid phosphatase in Arabidopsis thaliana moderates carbon metabolism and its overexpression leads to faster plant growth and higher seed yield
Authors
Issue Date2012
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPH
Citation
New Phytologist, 2012, v. 194 n. 1, p. 206-219 How to Cite?
Abstract
* Overexpression of AtPAP2, a purple acid phosphatase (PAP) with a unique C-terminal hydrophobic motif in Arabidopsis, resulted in earlier bolting and a higher seed yield. Metabolite analysis showed that the shoots of AtPAP2 overexpression lines contained higher levels of sugars and tricarboxylic acid (TCA) metabolites. Enzyme assays showed that sucrose phosphate synthase (SPS) activity was significantly upregulated in the overexpression lines. The higher SPS activity arose from a higher level of SPS protein, and was independent of SnRK1. * AtPAP2 was found to be targeted to both plastids and mitochondria via its C-terminal hydrophobic motif. Ectopic expression of a truncated AtPAP2 without this C-terminal motif in Arabidopsis indicated that the subcellular localization of AtPAP2 is essential for its biological actions. * Plant PAPs are generally considered to mediate phosphorus acquisition and redistribution. AtPAP2 is the first PAP shown to modulate carbon metabolism and the first shown to be dual-targeted to both plastids and mitochondria by a C-terminal targeting signal. * One PAP-like sequence carrying a hydrophobic C-terminal motif could be identified in the genome of the smallest free-living photosynthetic eukaryote, Ostreococcus tauri. This might reflect a common ancestral function of AtPAP2-like sequences in the regulation of carbon metabolism.
Persistent Identifierhttp://hdl.handle.net/10722/145622
ISSN
ISI Accession Number ID
Funding AgencyGrant Number
HKSAR, ChinaHKU772710M
ITS158/09
Funding Information:

This project was supported by the General Research Fund (HKU772710M) and the Innovation and Technology Fund (ITS158/09) of the HKSAR, China. We thank Dr Yip's lab at HKU for kindly providing plant vectors and technical support for plant cultures. We thank Aimee Llewellyn and Delia Corol at Rothamsted Research for preparation of the analytical extracts and for 1H-NMR data collection, Dr David Secco at the University of Western Australia for his comments on this manuscript.

 

DC FieldValueLanguage
dc.contributor.authorSun, Fen_US
dc.contributor.authorSuen, PKen_US
dc.contributor.authorZhang, Yen_US
dc.contributor.authorLiang, Cen_US
dc.contributor.authorCarrie, Cen_US
dc.contributor.authorWhelan, Jen_US
dc.contributor.authorWard, JLen_US
dc.contributor.authorHawkins, NDen_US
dc.contributor.authorJiang, Len_US
dc.contributor.authorLim, BLen_US
dc.date.accessioned2012-02-28T01:58:40Z-
dc.date.available2012-02-28T01:58:40Z-
dc.date.issued2012en_US
dc.identifier.citationNew Phytologist, 2012, v. 194 n. 1, p. 206-219en_US
dc.identifier.issn0028-646Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/145622-
dc.description.abstract* Overexpression of AtPAP2, a purple acid phosphatase (PAP) with a unique C-terminal hydrophobic motif in Arabidopsis, resulted in earlier bolting and a higher seed yield. Metabolite analysis showed that the shoots of AtPAP2 overexpression lines contained higher levels of sugars and tricarboxylic acid (TCA) metabolites. Enzyme assays showed that sucrose phosphate synthase (SPS) activity was significantly upregulated in the overexpression lines. The higher SPS activity arose from a higher level of SPS protein, and was independent of SnRK1. * AtPAP2 was found to be targeted to both plastids and mitochondria via its C-terminal hydrophobic motif. Ectopic expression of a truncated AtPAP2 without this C-terminal motif in Arabidopsis indicated that the subcellular localization of AtPAP2 is essential for its biological actions. * Plant PAPs are generally considered to mediate phosphorus acquisition and redistribution. AtPAP2 is the first PAP shown to modulate carbon metabolism and the first shown to be dual-targeted to both plastids and mitochondria by a C-terminal targeting signal. * One PAP-like sequence carrying a hydrophobic C-terminal motif could be identified in the genome of the smallest free-living photosynthetic eukaryote, Ostreococcus tauri. This might reflect a common ancestral function of AtPAP2-like sequences in the regulation of carbon metabolism.-
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPHen_US
dc.relation.ispartofNew Phytologisten_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong Licenseen_US
dc.subject.meshAcid Phosphatase - chemistry - metabolism-
dc.subject.meshArabidopsis - drug effects - enzymology - growth and development-
dc.subject.meshArabidopsis Proteins - chemistry - metabolism-
dc.subject.meshGlycoproteins - chemistry - metabolism-
dc.subject.meshSeeds - drug effects - growth and development-
dc.titleA dual-targeted purple acid phosphatase in Arabidopsis thaliana moderates carbon metabolism and its overexpression leads to faster plant growth and higher seed yielden_US
dc.typeArticleen_US
dc.identifier.emailSuen, PK: ericsuen@hku.hken_US
dc.identifier.emailLim, BL: bllim@hku.hken_US
dc.identifier.authorityLim, BL=rp00744en_US
dc.description.naturepreprint-
dc.identifier.doi10.1111/j.1469-8137.2011.04026.x-
dc.identifier.pmid22269069-
dc.identifier.scopuseid_2-s2.0-84862777582-
dc.identifier.hkuros198745en_US
dc.identifier.volume194-
dc.identifier.issue1-
dc.identifier.spage206-
dc.identifier.epage219-
dc.identifier.eissn1469-8137-
dc.identifier.isiWOS:000300719400021-
dc.publisher.placeUnited Kingdom-

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