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dc.contributor.author
Bustos, Diego Martin  
dc.contributor.author
Bustamante, Claudia Anabel  
dc.contributor.author
Iglesias, Alberto Alvaro  
dc.date.available
2019-10-09T17:54:59Z  
dc.date.issued
2008-03  
dc.identifier.citation
Bustos, Diego Martin; Bustamante, Claudia Anabel; Iglesias, Alberto Alvaro; Involvement of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in response to oxidative stress; Elsevier Gmbh; Journal of Plant Physiology; 165; 4; 3-2008; 456-461  
dc.identifier.issn
0176-1617  
dc.identifier.uri
http://hdl.handle.net/11336/85467  
dc.description.abstract
Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Because non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (NP-Ga3PDHase) is involved in the production of reductive power (NADPH) in the cytosol, its behavior under oxidative stress conditions was analyzed. The specific activity of the enzyme was found to increase up to 2-fold after oxidative conditions imposed by methylviologen in wheat and maize seedlings. Under moderate oxidant concentration, lack of mRNA induction was observed. The increase in specific activity would thus be a consequence of a significant stability of NP-Ga3PDHase. Our results suggest that the enzyme could be modified by oxidation of cysteine residues, but formation of disulfide bridges is dependent on levels of divalent cations and 14-3-3 proteins. The latter differential effect could be critical to relatively maintain energy and reductant levels in the cytoplasm of plant cells under oxidative stress.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Gmbh  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
NP-GA3PDHASE ACTIVITY  
dc.subject
OXIDATIVE STRESS  
dc.subject
PROTEIN STABILITY  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Involvement of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in response to oxidative stress  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-09-27T14:16:45Z  
dc.journal.volume
165  
dc.journal.number
4  
dc.journal.pagination
456-461  
dc.journal.pais
Alemania  
dc.journal.ciudad
Berlín  
dc.description.fil
Fil: Bustos, Diego Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina  
dc.description.fil
Fil: Bustamante, Claudia Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina  
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Enzimología Molecular; Argentina  
dc.journal.title
Journal of Plant Physiology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jplph.2007.06.005  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0176161707001332