Show simple item record

Title

Structural basis for redox regulation of cytoplasmic and chloroplastic triosephosphate isomerases from Arabidopsis thaliana

dc.contributor.authorLópez Castillo, Laura Margarita
dc.contributor.authorJiménez Sandoval, Pedro
dc.contributor.authorBaruch Torres, Noe
dc.contributor.authorTrasviña Arenas, Carlos Humberto
dc.contributor.authorDíaz Quezada, Corina
dc.contributor.authorLara González, Samuel
dc.contributor.authorWinkler, Robert
dc.contributor.authorBrieba, Luis G
dc.date.accessioned2018-03-23T23:59:24Z
dc.date.available2018-03-23T23:59:24Z
dc.date.issued2016-12
dc.identifier.citationLópez-Castillo LM, Jiménez-Sandoval P, Baruch-Torres N, Trasviña-Arenas CH, Díaz-Quezada C, Lara-González S, Winkler R and Brieba LG (2016) Structural Basis for Redox Regulation of Cytoplasmic and Chloroplastic Triosephosphate Isomerases from Arabidopsis thaliana. Front. Plant Sci. 7:1817. doi: 10.3389/fpls.2016.01817
dc.identifier.urihttp://hdl.handle.net/11627/3685
dc.description.abstract"In plants triosephosphate isomerase (TPI) interconyerts glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) during glycolysis, gluconeogenesis, and the Calvin-Benson cycle. The nuclear genome of land plants encodes two tpi genes, one gene product is located in the cytoplasm and the other is imported into the chloroplast. Herein we report the crystal structures of the TPIs from the vascular plant Arabidopsis thaliana (AtTPIs) and address their enzymatic modulation by redox agents. Cytoplasmic TPI (cTPI) and chloroplast TPI (pdTPI) share more than 60% amino acid identity and assemble as (beta-alpha)(8) dimers with high structural homology. cTPI and pdTPI harbor two and one accessible thiol groups per monomer respectively. cTPI and pdTPI present a cysteine at an equivalent structural position (C13 and C15 respectively) and cTPI also contains a specific solvent accessible cysteine at residue 218 (cTPI-C218). Site directed mutagenesis of residues pdTPI-C15, cTPI-C13, and cTPI-C218 to serine substantially decreases enzymatic activity, indicating that the structural integrity of these cysteines is necessary for catalysis. AtTPIs exhibit differential responses to oxidative agents, cTPI is susceptible to oxidative agents such as diamide and H2O2, whereas pdTPI is resistant to inhibition. Incubation of AtTPIs with the sulfhydryl conjugating reagents methylmethane thiosulfonate (MMTS) and glutathione inhibits enzymatic activity. However, the concentration necessary to inhibit pdTPI is at least two orders of magnitude higher than the concentration needed to inhibit cTPI. Western-blot analysis indicates that residues cTPI-C13, cTPI-C218, and pdTPI-C15 conjugate with glutathione. In summary, our data indicate that AtTPIs could be redox regulated by the derivatization of specific AtTPI cysteines (cTPI-C13 and pdTPI-C15 and cTPI-C218). Since AtTPIs have evolved by gene duplication, the higher resistance of pdTPI to redox agents may be an adaptive consequence to the redox environment in the chloroplast."
dc.publisherFrontiers Media S.A.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectTriosephosphate isomerase
dc.subjectArabidopsis thaliana
dc.subjectX-ray structure
dc.subjectThiol-based redox regulation
dc.subjectGlutathionylation
dc.subject.classificationBIOLOGÍA MOLECULAR
dc.titleStructural basis for redox regulation of cytoplasmic and chloroplastic triosephosphate isomerases from Arabidopsis thaliana
dc.typearticle
dc.identifier.doihttps://doi.org/10.3389/fpls.2016.01817
dc.rights.accessAcceso Abierto


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivatives 4.0 Internacional