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dc.contributor.author
Camargo, Ana I.
dc.contributor.author
Wiggers, Helton J.
dc.contributor.author
Damalio, Julio C. P.
dc.contributor.author
Araujo, Ana P. U.
dc.contributor.author
Ribichich, Karina Fabiana
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dc.contributor.author
Camargo, Paulo C. de
dc.date.available
2017-09-01T19:07:08Z
dc.date.issued
2013-12
dc.identifier.citation
Camargo, Ana I.; Wiggers, Helton J.; Damalio, Julio C. P.; Araujo, Ana P. U.; Ribichich, Karina Fabiana; et al.; Structural and thermodynamic studies of two centrin isoforms from Blastocladiella emersonii upon calcium binding; Elsevier; Biochimica Et Biophysica Acta-proteins And Proteomics; 1834; 12; 12-2013; 2823-2831
dc.identifier.issn
1570-9639
dc.identifier.uri
http://hdl.handle.net/11336/23467
dc.description.abstract
Centrins are calcium-binding proteins associated with microtubules organizing centers. Members of two divergent subfamilies of centrins were found in the aquatic fungus Blastocladiella emersonii, contrasting with the occurrence of only one member known for the better explored terrestrial fungi. BeCen1, shows greatest identity with human centrins HsCen1, HsCen2 and green algae centrin CrCenp, while BeCen3 records largest identity with human centrin HsCen3 and yeast centrin Cdc31p. Following the discovery of this unique feature, BeCen1 and BeCen3 centrins were produced to study whether these proteins had distinct features upon calcium binding. Circular dichroism showed opposite calcium binding effects on the alpha-helix arrangement of the secondary structure. The spectra indicated a decrease in alpha-helix signal for holo-BeCen1 contrasting with an increase for holo-BeCen3. In addition, only BeCen1 refolds after being denatured. The fluorescence emission of the hydrophobic probe ANS increases for both proteins likely due to hydrophobic exposure, however, only BeCen1 presents a clear blue shift when calcium is added. ITC experiments identified four calcium binding sites for both proteins. In contrast to calcium binding to BeCen1, which is mainly endothermic, binding to BeCen3 is mainly exothermic. Light-scattering evidenced the formation of large particles in solution for BeCen1 and BeCen3 at temperatures above 30°C and 40°C, respectively. Atomic force microscopy confirmed the presence of supramolecular structures, which differ in the compactness and branching degree. Binding of calcium leads to different structural changes in BeCen1 und BeCen3 and the thermodynamic characteristics of the interaction also differ.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Centrins
dc.subject
Blastocladiella Emersonii
dc.subject
Calcium-Binding Protein
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Ef-Hand Protein
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Isothermal Titration Calorimetry (Itc)
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Structural and thermodynamic studies of two centrin isoforms from Blastocladiella emersonii upon calcium binding
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-08-24T18:47:05Z
dc.journal.volume
1834
dc.journal.number
12
dc.journal.pagination
2823-2831
dc.journal.pais
Países Bajos
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dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Camargo, Ana I.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Wiggers, Helton J.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Damalio, Julio C. P.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Araujo, Ana P. U.. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Ribichich, Karina Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Camargo, Paulo C. de. Universidade Federal do Paraná; Brasil
dc.journal.title
Biochimica Et Biophysica Acta-proteins And Proteomics
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1570963913003658
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbapap.2013.10.007
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