Correlation between fluorescence and structure in the orange-emitting GFP-like protein, monomeric Kusabira Orange.
Identifieur interne : 000299 ( PubMed/Curation ); précédent : 000298; suivant : 000300Correlation between fluorescence and structure in the orange-emitting GFP-like protein, monomeric Kusabira Orange.
Auteurs : A. Ausili [Italie] ; M. Staiano [Italie] ; A. Marabotti [Italie] ; G. D'Auria [Italie] ; J C G Mez-Fernández [Espagne] ; A. Torrecillas [Espagne] ; A. Ortiz [Espagne] ; S. D'Auria [Italie]Source :
- Journal of photochemistry and photobiology. B, Biology [ 1873-2682 ] ; 2014.
English descriptors
- KwdEn :
- Calorimetry, Differential Scanning, Citrus sinensis, Luminescent Proteins (chemistry), Luminescent Proteins (metabolism), Protein Denaturation, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrometry, Fluorescence, Spectroscopy, Fourier Transform Infrared, Temperature, Thermodynamics.
- MESH :
- chemical , chemistry : Luminescent Proteins.
- chemical , metabolism : Luminescent Proteins.
- Calorimetry, Differential Scanning, Citrus sinensis, Protein Denaturation, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrometry, Fluorescence, Spectroscopy, Fourier Transform Infrared, Temperature, Thermodynamics.
Abstract
The mKO is the monomeric version of Kusabira Orange, a GFP-like protein emitting bright orange fluorescence at 559 nm. This protein shows the characteristic β-barrel motif typical of the fluorescent protein family which it belongs to, similar spectral properties to the tetrameric form and an exceptional photo-stability to pH changes. Here, we demonstrate that mKO in solution at physiological pH exhibits a secondary structure analogue to that of the crystal. Moreover, we describe the thermal unfolding, revealing an outstanding structural stability with a denaturation temperature close to 90 °C and identifying the existence of a thermodynamic intermediate. The denaturation process of mKO results to be absolutely irreversible because of the complete lost of the native structure and the consequent aggregation, while the presence of the intermediate state is most likely due to coexistence of two different species of mKO, with protonated and deprotonated chromophore respectively, that affects the fluorescence properties and the structural stability of the protein.
DOI: 10.1016/j.jphotobiol.2014.04.028
PubMed: 24980638
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Marabotti</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry and Biology, University of Salerno, Fisciano (SA), Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry and Biology, University of Salerno, Fisciano (SA)</wicri:regionArea></affiliation></author><author><name sortKey="D Auria, G" sort="D Auria, G" uniqKey="D Auria G" first="G" last="D'Auria">G. D'Auria</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy; Department of Chemistry and Biology, University of Salerno, Fisciano (SA), Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy; Department of Chemistry and Biology, University of Salerno, Fisciano (SA)</wicri:regionArea></affiliation></author><author><name sortKey="G Mez Fernandez, J C" sort="G Mez Fernandez, J C" uniqKey="G Mez Fernandez J" first="J C" last="G Mez-Fernández">J C G Mez-Fernández</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia</wicri:regionArea></affiliation></author><author><name sortKey="Torrecillas, A" sort="Torrecillas, A" uniqKey="Torrecillas A" first="A" last="Torrecillas">A. Torrecillas</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia</wicri:regionArea></affiliation></author><author><name sortKey="Ortiz, A" sort="Ortiz, A" uniqKey="Ortiz A" first="A" last="Ortiz">A. Ortiz</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia</wicri:regionArea></affiliation></author><author><name sortKey="D Auria, S" sort="D Auria, S" uniqKey="D Auria S" first="S" last="D'Auria">S. D'Auria</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy. 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This protein shows the characteristic β-barrel motif typical of the fluorescent protein family which it belongs to, similar spectral properties to the tetrameric form and an exceptional photo-stability to pH changes. Here, we demonstrate that mKO in solution at physiological pH exhibits a secondary structure analogue to that of the crystal. Moreover, we describe the thermal unfolding, revealing an outstanding structural stability with a denaturation temperature close to 90 °C and identifying the existence of a thermodynamic intermediate. The denaturation process of mKO results to be absolutely irreversible because of the complete lost of the native structure and the consequent aggregation, while the presence of the intermediate state is most likely due to coexistence of two different species of mKO, with protonated and deprotonated chromophore respectively, that affects the fluorescence properties and the structural stability of the protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24980638</PMID><DateCreated><Year>2014</Year><Month>8</Month><Day>2</Day></DateCreated><DateCompleted><Year>2015</Year><Month>03</Month><Day>31</Day></DateCompleted><DateRevised><Year>2014</Year><Month>8</Month><Day>2</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2682</ISSN><JournalIssue CitedMedium="Internet"><Volume>138</Volume><PubDate><Year>2014</Year><Month>Sep</Month><Day>5</Day></PubDate></JournalIssue><Title>Journal of photochemistry and photobiology. B, Biology</Title><ISOAbbreviation>J. Photochem. Photobiol. B, Biol.</ISOAbbreviation></Journal><ArticleTitle>Correlation between fluorescence and structure in the orange-emitting GFP-like protein, monomeric Kusabira Orange.</ArticleTitle><Pagination><MedlinePgn>223-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jphotobiol.2014.04.028</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1011-1344(14)00136-5</ELocationID><Abstract><AbstractText>The mKO is the monomeric version of Kusabira Orange, a GFP-like protein emitting bright orange fluorescence at 559 nm. This protein shows the characteristic β-barrel motif typical of the fluorescent protein family which it belongs to, similar spectral properties to the tetrameric form and an exceptional photo-stability to pH changes. Here, we demonstrate that mKO in solution at physiological pH exhibits a secondary structure analogue to that of the crystal. Moreover, we describe the thermal unfolding, revealing an outstanding structural stability with a denaturation temperature close to 90 °C and identifying the existence of a thermodynamic intermediate. The denaturation process of mKO results to be absolutely irreversible because of the complete lost of the native structure and the consequent aggregation, while the presence of the intermediate state is most likely due to coexistence of two different species of mKO, with protonated and deprotonated chromophore respectively, that affects the fluorescence properties and the structural stability of the protein.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ausili</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy. Electronic address: a.ausili@ibp.cnr.it.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Staiano</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Marabotti</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Biology, University of Salerno, Fisciano (SA), Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>D'Auria</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy; Department of Chemistry and Biology, University of Salerno, Fisciano (SA), Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gómez-Fernández</LastName><ForeName>J C</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Torrecillas</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ortiz</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departamento de Bioquimica y Biologia Molecular-A, University of Murcia, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>D'Auria</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy. Electronic address: s.dauria@ibp.cnr.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>May</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>J Photochem Photobiol B</MedlineTA><NlmUniqueID>8804966</NlmUniqueID><ISSNLinking>1011-1344</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008164">Luminescent Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002152" MajorTopicYN="N">Calorimetry, Differential Scanning</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032084" MajorTopicYN="N">Citrus sinensis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008164" MajorTopicYN="N">Luminescent Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017550" MajorTopicYN="N">Spectroscopy, Fourier Transform Infrared</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">FTIR</Keyword><Keyword MajorTopicYN="N">Fluorescent proteins</Keyword><Keyword MajorTopicYN="N">Protein structure</Keyword><Keyword MajorTopicYN="N">Thermo-stability</Keyword><Keyword MajorTopicYN="N">mKO</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>2</Month><Day>3</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>4</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>7</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>4</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24980638</ArticleId><ArticleId IdType="pii">S1011-1344(14)00136-5</ArticleId><ArticleId IdType="doi">10.1016/j.jphotobiol.2014.04.028</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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