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dc.contributor.author
Ordoñez, Maria Victoria
dc.contributor.author
Guillén, J.
dc.contributor.author
Nercessian, Debora
dc.contributor.author
Villalaín, J.
dc.contributor.author
Conde, Ruben Danilo
dc.date.available
2017-02-16T13:43:29Z
dc.date.issued
2011-09
dc.identifier.citation
Ordoñez, Maria Victoria; Guillén, J.; Nercessian, Debora; Villalaín, J.; Conde, Ruben Danilo; Secondary structure determination by FTIR of an archaeal ubiquitin-like polypeptide from Natrialba magadii; Springer; European Biophysics Journal With Biophysics Letters; 40; 9; 9-2011; 1101-1107
dc.identifier.issn
0175-7571
dc.identifier.uri
http://hdl.handle.net/11336/13062
dc.description.abstract
The ubiquitin protein belongs to the β-grasp fold family, characterized by four or five β-sheets with a single α-helical middle region. Ubiquitin-like proteins (Ubls) are structural homologues with low sequence identity to ubiquitin and are widespread among both eukaryotes and prokaryotes. We previously demonstrated by bioinformatics that P400, a polypeptide from the haloalkaliphilic archaeon Natrialba magadii, has structural homology with both ubiquitin and Ubls. This work examines the secondary structure of P400 by Fourier transform infrared spectroscopy (FTIR). After expression in Escherichia coli, recombinant P400 (rP400) was separated by PAGE and eluted pure from zinc-imidazole reversely stained gels. The requirement of high salt concentration of this polypeptide to be folded was corroborated by intrinsic fluorescence spectrum. Our results show that fluorescence spectra of rP400 in 1.5 M KCl buffer shifts and decreases after thermal denaturation as well as after chemical treatment. rP400 was lyophilized and rehydrated in buffer containing 1.5 M KCl before both immunochemical and FTIR tests were performed. It was found that rP400 reacts with anti-ubiquitin antibody after rehydration in the presence of high salt concentrations. On the other hand, like ubiquitin and Ubls, the amide I′ band for rP400 shows 10% more of its sequence to be involved in β-sheet structures than in α-helix. These findings suggest that P400 is a structural homologue of the ubiquitin family proteins.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Halophilic Archaea
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Natrialba Magadii
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Ubiquitin-Like Proteins
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Beta-Grasp Fold
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Β-Grasp Fold
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Ftir
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Structural Homology
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Secondary structure determination by FTIR of an archaeal ubiquitin-like polypeptide from Natrialba magadii
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-02-13T20:24:30Z
dc.identifier.eissn
1432-1017
dc.journal.volume
40
dc.journal.number
9
dc.journal.pagination
1101-1107
dc.journal.pais
Alemania
dc.journal.ciudad
Berlín
dc.description.fil
Fil: Ordoñez, Maria Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
dc.description.fil
Fil: Guillén, J.. Universidad de Murcia. Facultad de Quimica. Dpto.de Bioqu.y Biolog.molecular E Inmunologia; España
dc.description.fil
Fil: Nercessian, Debora. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
dc.description.fil
Fil: Villalaín, J.. Universidad de Miguel Hernandez. Centro de Biologia Molecular y Celular; España
dc.description.fil
Fil: Conde, Ruben Danilo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
dc.journal.title
European Biophysics Journal With Biophysics Letters
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs00249-011-0719-y
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00249-011-0719-y
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