Structural basis for the modulation of plant cytosolic triosephosphate isomerase activity by mimicry of redox‐based modifications

Castro‐Torres, Eduardo; Jiménez‐Sandoval, Pedro; Romero‐Romero, Sergio; Fuentes‐Pascacio, Alma; López‐Castillo, Laura M.; Díaz‐Quezada, Corina; Fernández‐Velasco, D. Alejandro; Torres‐Larios, Alfredo; Brieba, Luis G.

doi:10.1111/tpj.14375

Title: Structural basis for the modulation of plant cytosolic triosephosphate isomerase activity by mimicry of redox‐based modifications

Journal Article · 13 June 2019 · The Plant Journal

DOI: https://doi.org/10.1111/tpj.14375 · OSTI ID:1526080

Castro‐Torres, Eduardo ^[1]; Jiménez‐Sandoval, Pedro ^[1]; Romero‐Romero, Sergio ^[2]; Fuentes‐Pascacio, Alma ^[1]; López‐Castillo, Laura M. ^[1]; Díaz‐Quezada, Corina ^[1]; Fernández‐Velasco, D. Alejandro ^[2]; Torres‐Larios, Alfredo ^[3];

^[1]

Laboratorio Nacional de Genómica para la Biodiversidad Centro de Investigación y de Estudios Avanzados del IPN Apartado Postal 629, Irapuato Guanajuato México CP 36821 México
Departamento de Bioquímica Facultad de Medicina Universidad Nacional Autónoma de México Circuito Exterior s/n Ciudad Universitaria Apartado Postal 70‐243 Mexico City 04510 México
Departamento de Bioquímica y Biología Estructural Instituto de Fisiología Celular Universidad Nacional Autónoma de México Circuito Exterior s/n Ciudad Universitaria Apartado Postal 70‐243 México City 04510 México

Summary Reactive oxidative species ( ROS ) and S‐ glutathionylation modulate the activity of plant cytosolic triosephosphate isomerases ( cTPI ). Arabidopsis thaliana cTPI (Atc TPI ) is subject of redox regulation at two reactive cysteines that function as thiol switches. Here we investigate the role of these residues, Atc TPI ‐Cys13 and At‐Cys218, by substituting them with aspartic acid that mimics the irreversible oxidation of cysteine to sulfinic acid and with amino acids that mimic thiol conjugation. Crystallographic studies show that mimicking Atc TPI ‐Cys13 oxidation promotes the formation of inactive monomers by reposition residue Phe75 of the neighboring subunit, into a conformation that destabilizes the dimer interface. Mutations in residue Atc TPI ‐Cys218 to Asp, Lys, or Tyr generate TPI variants with a decreased enzymatic activity by creating structural modifications in two loops (loop 7 and loop 6) whose integrity is necessary to assemble the active site. In contrast with mutations in residue Atc TPI ‐Cys13, mutations in Atc TPI ‐Cys218 do not alter the dimeric nature of Atc TPI . Therefore, modifications of residues Atc TPI ‐Cys13 and Atc TPI ‐Cys218 modulate Atc TPI activity by inducing the formation of inactive monomers and by altering the active site of the dimeric enzyme, respectively. The identity of residue Atc TPI ‐Cys218 is conserved in the majority of plant cytosolic TPI s, this conservation and its solvent‐exposed localization make it the most probable target for TPI regulation upon oxidative damage by reactive oxygen species. Our data reveal the structural mechanisms by which S ‐glutathionylation protects Atc TPI from irreversible chemical modifications and re‐routes carbon metabolism to the pentose phosphate pathway to decrease oxidative stress.

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Sponsoring Organization:: USDOE

OSTI ID:: 1526080

Journal Information:: The Plant Journal, Journal Name: The Plant Journal Journal Issue: 5 Vol. 99; ISSN 0960-7412

Publisher:: Wiley-BlackwellCopyright Statement

Country of Publication:: United Kingdom

Language:: English

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