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dc.contributor.author
de Pino, Veronica
dc.contributor.author
Marino, Cristina Ester
dc.contributor.author
Moreno, Silvia
dc.date.available
2017-03-31T14:36:55Z
dc.date.issued
2012-02
dc.identifier.citation
de Pino, Veronica; Marino, Cristina Ester; Moreno, Silvia; Oligomerization of the reversibly glycosylated polypeptide: its role during rice plant development and in the regulation of self-glycosylation; Springer; Protoplasma; 250; 1; 2-2012; 111-119
dc.identifier.issn
0033-183X
dc.identifier.uri
http://hdl.handle.net/11336/14580
dc.description.abstract
A multigenic family of self-glycosylating proteins named reversibly glycosylated polypeptides, designated as RGPs, have been usually associated with carbohydrate metabolism, although they are an enigma both at the functional, as well as at the structural level. In this work, we used biochemical approaches to demonstrate that complex formation is linked to rice plant development, in which class 1 Oryza sativa RGP (OsRGP) would be involved in an early stage of growing plants, while class 2 OsRGP would be associated with a late stage linked to an active polysaccharide synthesis that occurs during the elongation of plant. Here, a further investigation of the complex formation of the Solanum tuberosum RGP (StRGP) was performed. Results showed that disulfide bonds are at least partially responsible for maintaining the oligomeric protein structure, so that the nonreduced StRGP protein showed an apparent higher molecular weight and a lower radioglycosylation of the monomer with respect to its reduced form. Hydrophobic cluster analysis and secondary structure prediction revealed that class 2 RGPs no longer maintained the Rossman fold described for class 1 RGP. A 3D structure of the StRGP protein resolved by homology modeling supports the possibility of intercatenary disulfide bridges formed by exposed cysteines residues C79, C303 and C251 and they are most probably involved in complex formation occurring into the cell cytoplasm.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Complex Formation
dc.subject
Plant Polysaccharide
dc.subject
Self-Glycosylation
dc.subject
Reversibly Glycosylated Polypeptide
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Oligomerization of the reversibly glycosylated polypeptide: its role during rice plant development and in the regulation of self-glycosylation
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-03-27T17:41:43Z
dc.journal.volume
250
dc.journal.number
1
dc.journal.pagination
111-119
dc.journal.pais
Austria
dc.journal.ciudad
Viena
dc.description.fil
Fil: de Pino, Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco (i); Argentina; Argentina
dc.description.fil
Fil: Marino, Cristina Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
dc.description.fil
Fil: Moreno, Silvia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
dc.journal.title
Protoplasma
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs00709-012-0382-x
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00709-012-0382-x
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