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Article: Spectral profiling for the simultaneous observation of four distinct fluorescent proteins and detection of protein-protein interaction via fluorescence resonance energy transfer in tobacco leaf nuclei

TitleSpectral profiling for the simultaneous observation of four distinct fluorescent proteins and detection of protein-protein interaction via fluorescence resonance energy transfer in tobacco leaf nuclei
Authors
Issue Date2002
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 2002, v. 129 n. 3, p. 931-942 How to Cite?
AbstractThe control of subcellular localization of proteins and their interaction with other partners in vivo are important parameters that provide clues to their function and regulation. The ability to simultaneously track multiple protein species with high resolution should provide a valuable assay system to study and characterize various types of posttranslational control pathways. In this work, we established the system and a method involving 'spectral profiling' for the resolution of four different fluorescent protein tags in the same viewing field using digital imaging technology. With these techniques, we have (a) developed new derivatives of mGFP5, which is commonly used in the plant field, that are about three times brighter; (b) demonstrated that four spectrally distinct fluorescent proteins (cyan, green, yellow, and red) that are fused to a transcription factor could be stably expressed in nuclei and distinguished in tobacco (Nicotiana tabacum) mesophyll cells; and (c) shown that interaction between partners of a dimeric transcription factor can be detected by measuring fluorescence resonance energy transfer. These technologies should help one to study protein-protein interactions efficiently, especially for nuclear proteins under in vivo conditions.
Persistent Identifierhttp://hdl.handle.net/10722/49003
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKato, Nen_HK
dc.contributor.authorPontier, Den_HK
dc.contributor.authorLam, Een_HK
dc.date.accessioned2008-06-12T06:31:53Z-
dc.date.available2008-06-12T06:31:53Z-
dc.date.issued2002en_HK
dc.identifier.citationPlant Physiology, 2002, v. 129 n. 3, p. 931-942en_HK
dc.identifier.issn0032-0889en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49003-
dc.description.abstractThe control of subcellular localization of proteins and their interaction with other partners in vivo are important parameters that provide clues to their function and regulation. The ability to simultaneously track multiple protein species with high resolution should provide a valuable assay system to study and characterize various types of posttranslational control pathways. In this work, we established the system and a method involving 'spectral profiling' for the resolution of four different fluorescent protein tags in the same viewing field using digital imaging technology. With these techniques, we have (a) developed new derivatives of mGFP5, which is commonly used in the plant field, that are about three times brighter; (b) demonstrated that four spectrally distinct fluorescent proteins (cyan, green, yellow, and red) that are fused to a transcription factor could be stably expressed in nuclei and distinguished in tobacco (Nicotiana tabacum) mesophyll cells; and (c) shown that interaction between partners of a dimeric transcription factor can be detected by measuring fluorescence resonance energy transfer. These technologies should help one to study protein-protein interactions efficiently, especially for nuclear proteins under in vivo conditions.en_HK
dc.format.extent388 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.orgen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshCell Nucleus - metabolismen_HK
dc.subject.meshLuminescent Proteins - genetics - metabolismen_HK
dc.subject.meshSpectrometry, Fluorescence - methodsen_HK
dc.subject.meshTobacco - genetics - metabolismen_HK
dc.subject.meshTranscription Factors - genetics - metabolismen_HK
dc.titleSpectral profiling for the simultaneous observation of four distinct fluorescent proteins and detection of protein-protein interaction via fluorescence resonance energy transfer in tobacco leaf nucleien_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0032-0889&volume=129&issue=3&spage=931&epage=942&date=2002&atitle=Spectral+profiling+for+the+simultaneous+observation+of+four+distinct+fluorescent+proteins+and+detection+of+protein-protein+interaction+via+fluorescence+resonance+energy+transfer+in+tobacco+leaf+nucleien_HK
dc.identifier.emailLam, E: ericl89@hotmail.comen_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1104/pp.005496en_HK
dc.identifier.pmid12114548-
dc.identifier.pmcidPMC1540237en_HK
dc.identifier.scopuseid_2-s2.0-0035984025-
dc.identifier.hkuros96618-
dc.identifier.isiWOS:000177045000002-

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