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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
dc.subject.classification
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
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