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Title: Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin

Abstract

2-Cys peroxiredoxin (2-Cys Prx) is a large group of proteins that participate in cell proliferation, differentiation, apoptosis, and photosynthesis. In the prevailing view, this ubiquitous peroxidase poises the concentration of H{sub 2}O{sub 2} and, in so doing, regulates signal transduction pathways or protects macromolecules against oxidative damage. Here, we describe First purification of 2-Cys Prx from higher plants and subsequently we show that the native and the recombinant forms of rapeseed leaves stimulate the activity of chloroplast fructose-1,6-bisphosphatase (CFBPase), a key enzyme of the photosynthetic CO{sub 2} assimilation. The absence of reductants, the strict requirement of both fructose 1,6-bisphosphate and Ca{sup 2+}, and the response of single mutants C174S and C179S CFBPase bring forward clear differences with the well-known stimulation mediated by reduced thioredoxin via the regulatory 170's loop of CFBPase. Taken together, these findings provide an unprecedented insight into chloroplast enzyme regulation wherein both 2-Cys Prx and the 170's loop of CFBPase exhibit novel functions.

Authors:
 [1];  [1];  [1];  [1];  [1];  [2]
  1. Instituto Leloir, Patricias Argentinas 435, C1405BWE Buenos Aires (Argentina)
  2. Instituto Leloir, Patricias Argentinas 435, C1405BWE Buenos Aires (Argentina). E-mail: rwolosiuk@leloir.org.ar
Publication Date:
OSTI Identifier:
20979876
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 355; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2007.02.013; PII: S0006-291X(07)00284-7; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; APOPTOSIS; BRASSICA; CALCIUM IONS; CARBON DIOXIDE; CELL PROLIFERATION; CHLOROPLASTS; FRUCTOSE; HYDROGEN PEROXIDE; METALS; MUTANTS; OXIDATION; PEROXIDASES; PHOTOSYNTHESIS

Citation Formats

Caporaletti, Daniel, D'Alessio, Ana C., Rodriguez-Suarez, Roberto J., Senn, Alejandro M., Duek, Paula D., and Wolosiuk, Ricardo A. Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.02.013.
Caporaletti, Daniel, D'Alessio, Ana C., Rodriguez-Suarez, Roberto J., Senn, Alejandro M., Duek, Paula D., & Wolosiuk, Ricardo A. Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin. United States. doi:10.1016/j.bbrc.2007.02.013.
Caporaletti, Daniel, D'Alessio, Ana C., Rodriguez-Suarez, Roberto J., Senn, Alejandro M., Duek, Paula D., and Wolosiuk, Ricardo A. Fri . "Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin". United States. doi:10.1016/j.bbrc.2007.02.013.
@article{osti_20979876,
title = {Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin},
author = {Caporaletti, Daniel and D'Alessio, Ana C. and Rodriguez-Suarez, Roberto J. and Senn, Alejandro M. and Duek, Paula D. and Wolosiuk, Ricardo A.},
abstractNote = {2-Cys peroxiredoxin (2-Cys Prx) is a large group of proteins that participate in cell proliferation, differentiation, apoptosis, and photosynthesis. In the prevailing view, this ubiquitous peroxidase poises the concentration of H{sub 2}O{sub 2} and, in so doing, regulates signal transduction pathways or protects macromolecules against oxidative damage. Here, we describe First purification of 2-Cys Prx from higher plants and subsequently we show that the native and the recombinant forms of rapeseed leaves stimulate the activity of chloroplast fructose-1,6-bisphosphatase (CFBPase), a key enzyme of the photosynthetic CO{sub 2} assimilation. The absence of reductants, the strict requirement of both fructose 1,6-bisphosphate and Ca{sup 2+}, and the response of single mutants C174S and C179S CFBPase bring forward clear differences with the well-known stimulation mediated by reduced thioredoxin via the regulatory 170's loop of CFBPase. Taken together, these findings provide an unprecedented insight into chloroplast enzyme regulation wherein both 2-Cys Prx and the 170's loop of CFBPase exhibit novel functions.},
doi = {10.1016/j.bbrc.2007.02.013},
journal = {Biochemical and Biophysical Research Communications},
number = 3,
volume = 355,
place = {United States},
year = {Fri Apr 13 00:00:00 EDT 2007},
month = {Fri Apr 13 00:00:00 EDT 2007}
}