A Cytosolic Bypass and G6P Shunt in Plants Lacking Peroxisomal Hydroxypyruvate Reductase
Abstract
The oxygenation of ribulose 1,5-bisphosphate by Rubisco is the first step in photorespiration and reduces the efficiency of photosynthesis in C3 plants. Our recent data indicate that mutants in photorespiration have increased rates of photosynthetic cyclic electron flow around photosystem I. We investigated mutant lines lacking peroxisomal hydroxypyruvate reductase to determine if there are connections between 2-phosphoglycolate accumulation and cyclic electron flow in Arabidopsis (Arabidopsis thaliana). We found that 2-phosphoglycolate is a competitive inhibitor of triose phosphate isomerase, an enzyme in the Calvin-Benson cycle that converts glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. This block in metabolism could be overcome if glyceraldehyde 3-phosphate is exported to the cytosol, where cytosolic triose phosphate isomerase could convert it to dihydroxyacetone phosphate. We found evidence that carbon is reimported as glucose-6-phosphate, forming a cytosolic bypass around the block of stromal triose phosphate isomerase. However, this also stimulates a glucose-6-phosphate shunt, which consumes ATP, which can be compensated by higher rates of cyclic electron flow.
- Authors:
-
- Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824
- Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824
- Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824
- Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, Plant Resilience Institute, Michigan State University, East Lansing, Michigan 48824
- Publication Date:
- Research Org.:
- Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1524250
- Alternate Identifier(s):
- OSTI ID: 1607882
- Grant/Contract Number:
- FG02-91ER2002; FG02-91ER20021
- Resource Type:
- Published Article
- Journal Name:
- Plant Physiology (Bethesda)
- Additional Journal Information:
- Journal Name: Plant Physiology (Bethesda) Journal Volume: 180 Journal Issue: 2; Journal ID: ISSN 0032-0889
- Publisher:
- American Society of Plant Biologists
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Li, Jiying, Weraduwage, Sarathi M., Preiser, Alyssa L., Tietz, Stefanie, Weise, Sean E., Strand, Deserah D., Froehlich, John E., Kramer, David M., Hu, Jianping, and Sharkey, Thomas D. A Cytosolic Bypass and G6P Shunt in Plants Lacking Peroxisomal Hydroxypyruvate Reductase. United States: N. p., 2019.
Web. doi:10.1104/pp.19.00256.
Li, Jiying, Weraduwage, Sarathi M., Preiser, Alyssa L., Tietz, Stefanie, Weise, Sean E., Strand, Deserah D., Froehlich, John E., Kramer, David M., Hu, Jianping, & Sharkey, Thomas D. A Cytosolic Bypass and G6P Shunt in Plants Lacking Peroxisomal Hydroxypyruvate Reductase. United States. https://doi.org/10.1104/pp.19.00256
Li, Jiying, Weraduwage, Sarathi M., Preiser, Alyssa L., Tietz, Stefanie, Weise, Sean E., Strand, Deserah D., Froehlich, John E., Kramer, David M., Hu, Jianping, and Sharkey, Thomas D. Mon .
"A Cytosolic Bypass and G6P Shunt in Plants Lacking Peroxisomal Hydroxypyruvate Reductase". United States. https://doi.org/10.1104/pp.19.00256.
@article{osti_1524250,
title = {A Cytosolic Bypass and G6P Shunt in Plants Lacking Peroxisomal Hydroxypyruvate Reductase},
author = {Li, Jiying and Weraduwage, Sarathi M. and Preiser, Alyssa L. and Tietz, Stefanie and Weise, Sean E. and Strand, Deserah D. and Froehlich, John E. and Kramer, David M. and Hu, Jianping and Sharkey, Thomas D.},
abstractNote = {The oxygenation of ribulose 1,5-bisphosphate by Rubisco is the first step in photorespiration and reduces the efficiency of photosynthesis in C3 plants. Our recent data indicate that mutants in photorespiration have increased rates of photosynthetic cyclic electron flow around photosystem I. We investigated mutant lines lacking peroxisomal hydroxypyruvate reductase to determine if there are connections between 2-phosphoglycolate accumulation and cyclic electron flow in Arabidopsis (Arabidopsis thaliana). We found that 2-phosphoglycolate is a competitive inhibitor of triose phosphate isomerase, an enzyme in the Calvin-Benson cycle that converts glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. This block in metabolism could be overcome if glyceraldehyde 3-phosphate is exported to the cytosol, where cytosolic triose phosphate isomerase could convert it to dihydroxyacetone phosphate. We found evidence that carbon is reimported as glucose-6-phosphate, forming a cytosolic bypass around the block of stromal triose phosphate isomerase. However, this also stimulates a glucose-6-phosphate shunt, which consumes ATP, which can be compensated by higher rates of cyclic electron flow.},
doi = {10.1104/pp.19.00256},
journal = {Plant Physiology (Bethesda)},
number = 2,
volume = 180,
place = {United States},
year = {Mon Mar 18 00:00:00 EDT 2019},
month = {Mon Mar 18 00:00:00 EDT 2019}
}
https://doi.org/10.1104/pp.19.00256
Web of Science