File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Molecular and biochemical characterization of AtPAP15, a purple acid phosphatase with phytase activity, in Arabidopsis

TitleMolecular and biochemical characterization of AtPAP15, a purple acid phosphatase with phytase activity, in Arabidopsis
Authors
Issue Date2009
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 2009, v. 151 n. 1, p. 199-209 How to Cite?
AbstractPurple acid phosphatase (PAP) catalyzes the hydrolysis of phosphate monoesters and anhydrides to release phosphate within an acidic pH range. Among the 29 PAP-like proteins in Arabidopsis (Arabidopsis thaliana), AtPAP15 (At3g07130) displays a greater degree of amino acid identity with soybean (Glycine max; GmPHY) and tobacco (Nicotiana tabacum) PAP (NtPAP) with phytase activity than the other AtPAPs. In this study, transgenic Arabidopsis that expressed an AtPAP15 promoter:: b-glucuronidase (GUS) fusion protein showed that AtPAP15 expression was developmentally and temporally regulated, with strong GUS staining at the early stages of seedling growth and pollen germination. The expression was also organ/tissue specific, with strongest GUS staining in the vasculature, pollen grains, and roots. The recombinant AtPAP purified from transgenic tobacco exhibited broad substrate specificity with moderate phytase activity. AtPAP15 T-DNA insertion lines exhibited a lower phytase and phosphatase activity in seedling and germinating pollen and lower pollen germination rate compared with the wild type and their complementation lines. Therefore, AtPAP15 likely mobilizes phosphorus reserves in plants, particularly during seed and pollen germination. Since AtPAP15 is not expressed in the root hair or in the epidermal cells, it is unlikely to play any role in external phosphorus assimilation. © 2009 American Society of Plant Biologists.
Persistent Identifierhttp://hdl.handle.net/10722/179157
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKuang, Ren_US
dc.contributor.authorChan, KHen_US
dc.contributor.authorYeung, Een_US
dc.contributor.authorLim, BLen_US
dc.date.accessioned2012-12-19T09:52:26Z-
dc.date.available2012-12-19T09:52:26Z-
dc.date.issued2009en_US
dc.identifier.citationPlant Physiology, 2009, v. 151 n. 1, p. 199-209en_US
dc.identifier.issn0032-0889en_US
dc.identifier.urihttp://hdl.handle.net/10722/179157-
dc.description.abstractPurple acid phosphatase (PAP) catalyzes the hydrolysis of phosphate monoesters and anhydrides to release phosphate within an acidic pH range. Among the 29 PAP-like proteins in Arabidopsis (Arabidopsis thaliana), AtPAP15 (At3g07130) displays a greater degree of amino acid identity with soybean (Glycine max; GmPHY) and tobacco (Nicotiana tabacum) PAP (NtPAP) with phytase activity than the other AtPAPs. In this study, transgenic Arabidopsis that expressed an AtPAP15 promoter:: b-glucuronidase (GUS) fusion protein showed that AtPAP15 expression was developmentally and temporally regulated, with strong GUS staining at the early stages of seedling growth and pollen germination. The expression was also organ/tissue specific, with strongest GUS staining in the vasculature, pollen grains, and roots. The recombinant AtPAP purified from transgenic tobacco exhibited broad substrate specificity with moderate phytase activity. AtPAP15 T-DNA insertion lines exhibited a lower phytase and phosphatase activity in seedling and germinating pollen and lower pollen germination rate compared with the wild type and their complementation lines. Therefore, AtPAP15 likely mobilizes phosphorus reserves in plants, particularly during seed and pollen germination. Since AtPAP15 is not expressed in the root hair or in the epidermal cells, it is unlikely to play any role in external phosphorus assimilation. © 2009 American Society of Plant Biologists.en_US
dc.languageengen_US
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.orgen_US
dc.relation.ispartofPlant Physiologyen_US
dc.subject.meshAcid Phosphatase - Genetics - Metabolismen_US
dc.subject.meshArabidopsis - Enzymologyen_US
dc.subject.meshArabidopsis Proteins - Genetics - Metabolismen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshDna, Bacterial - Geneticsen_US
dc.subject.meshGene Expression Regulation, Enzymologic - Physiologyen_US
dc.subject.meshGene Expression Regulation, Plant - Physiologyen_US
dc.subject.meshGenetic Complementation Testen_US
dc.subject.meshMultienzyme Complexes - Genetics - Metabolismen_US
dc.subject.meshMutagenesis, Insertionalen_US
dc.subject.meshMutationen_US
dc.subject.meshPlants, Genetically Modifieden_US
dc.subject.meshSubstrate Specificityen_US
dc.subject.meshTobacco - Geneticsen_US
dc.titleMolecular and biochemical characterization of AtPAP15, a purple acid phosphatase with phytase activity, in Arabidopsisen_US
dc.typeArticleen_US
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_US
dc.identifier.authorityLim, BL=rp00744en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1104/pp.109.143180en_US
dc.identifier.pmid19633233-
dc.identifier.pmcidPMC2735976-
dc.identifier.scopuseid_2-s2.0-70349209373en_US
dc.identifier.hkuros164336-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-70349209373&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume151en_US
dc.identifier.issue1en_US
dc.identifier.spage199en_US
dc.identifier.epage209en_US
dc.identifier.eissn1532-2548-
dc.identifier.isiWOS:000269522200016-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridKuang, R=41361483500en_US
dc.identifier.scopusauthoridChan, KH=41361030400en_US
dc.identifier.scopusauthoridYeung, E=7101971768en_US
dc.identifier.scopusauthoridLim, BL=7201983917en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats