dc.creator | Alvarez, Clarisa Ester | |
dc.creator | Detarsio, Enrique | |
dc.creator | Moreno, Silvia Margarita | |
dc.creator | Andreo, Carlos Santiago | |
dc.creator | Drincovich, Maria Fabiana | |
dc.date.accessioned | 2018-10-01T15:35:39Z | |
dc.date.accessioned | 2018-11-06T12:18:08Z | |
dc.date.available | 2018-10-01T15:35:39Z | |
dc.date.available | 2018-11-06T12:18:08Z | |
dc.date.created | 2018-10-01T15:35:39Z | |
dc.date.issued | 2012-06 | |
dc.identifier | Alvarez, Clarisa Ester; Detarsio, Enrique; Moreno, Silvia Margarita; Andreo, Carlos Santiago; Drincovich, Maria Fabiana; Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity; Oxford University Press; Plant And Cell Physiology; 53; 6; 6-2012; 1144-1153 | |
dc.identifier | 0032-0781 | |
dc.identifier | http://hdl.handle.net/11336/61354 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1865297 | |
dc.description.abstract | Two highly similar plastidic NADP-malic enzymes (NADP-MEs) are found in the C 4 species maize (Zea mays); one exclusively expressed in the bundle sheath cells (BSCs) and involved in C 4 photosynthesis (ZmC 4-NADP-ME); and the other (ZmnonC 4-NADP-ME) with housekeeping roles. In the present work, these two NADP-MEs were analyzed regarding their redox-dependent activity modulation. The results clearly show that ZmC 4-NADP-ME is the only one modulated by redox status, and that its oxidation produces a conformational change limiting the catalytic process, although inducing higher affinity binding of the substrates. The reversal of ZmC 4-NADP-ME oxidation by chemical reductants suggests the presence of thiol groups able to form disulfide bonds. In order to identify the cysteine residues involved in the activity modulation, site-directed mutagenesis and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis of ZmC 4-NADP-ME were performed. The results obtained allowed the identification of Cys192, Cys246 (not conserved in ZmnonC 4-NADP-ME), Cys270 and Cys410 as directly or indirectly implicated in ZmC 4-NADP-ME redox modulation. These residues may be involved in forming disulfide bridge(s) or in the modulation of the oxidation of critical residues. Overall, the results indicate that, besides having acquired a high level of expression and localization in BSCs, ZmC 4-NADP-ME displays a particular redox modulation, which may be required to accomplish the C 4 photosynthetic metabolism. Therefore, the present work could provide new insights into the regulatory mechanisms potentially involved in the recruitment of genes for the C 4 pathway during evolution. © 2012 The Author. | |
dc.language | eng | |
dc.publisher | Oxford University Press | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1093/pcp/pcs059 | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/pcp/article/53/6/1144/1809330 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | C 4 PHOTOSYNTHESIS | |
dc.subject | MAIZE | |
dc.subject | NADP-MALIC ENZYME | |
dc.subject | REDOX MODULATION | |
dc.subject | STRUCTURE-FUNCTION RELATIONSHIP | |
dc.title | Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-Malic enzyme activity | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |