Show simple item record Camargo, Ana I. Wiggers, Helton J. Damalio, Julio C. P. Araujo, Ana P. U. Ribichich, Karina Fabiana Camargo, Paulo C. de 2017-09-01T19:07:08Z 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.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
dc.rights info:eu-repo/semantics/restrictedAccess
dc.subject CENTRINS
dc.subject EF-HAND PROTEIN
dc.subject.classification Bioquímica y Biología Molecular
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
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 2017-08-24T18:47:05Z
dc.journal.volume 1834
dc.journal.number 12
dc.journal.pagination 2823-2831
dc.journal.pais Países Bajos
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
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/

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