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Matrix Redox Physiology Governs the Regulation of Plant Mitochondrial Metabolism through Posttranslational Protein Modifications

Møller, Ian Max ; Igamberdiev, Abir U. ; Bykova, Natalia V. ; Finkemeier, Iris ; Rasmusson, Allan G. LU and Schwarzländer, Markus (2020) In The Plant cell 32(3). p.573-594
Abstract

Mitochondria function as hubs of plant metabolism. Oxidative phosphorylation produces ATP, but it is also a central high-capacity electron sink required by many metabolic pathways that must be flexibly coordinated and integrated. Here, we review the crucial roles of redox-associated posttranslational protein modifications (PTMs) in mitochondrial metabolic regulation. We discuss several major concepts. First, the major redox couples in the mitochondrial matrix (NAD, NADP, thioredoxin, glutathione, and ascorbate) are in kinetic steady state rather than thermodynamic equilibrium. Second, targeted proteomics have produced long lists of proteins potentially regulated by Cys oxidation/thioredoxin, Met-SO formation, phosphorylation, or Lys... (More)

Mitochondria function as hubs of plant metabolism. Oxidative phosphorylation produces ATP, but it is also a central high-capacity electron sink required by many metabolic pathways that must be flexibly coordinated and integrated. Here, we review the crucial roles of redox-associated posttranslational protein modifications (PTMs) in mitochondrial metabolic regulation. We discuss several major concepts. First, the major redox couples in the mitochondrial matrix (NAD, NADP, thioredoxin, glutathione, and ascorbate) are in kinetic steady state rather than thermodynamic equilibrium. Second, targeted proteomics have produced long lists of proteins potentially regulated by Cys oxidation/thioredoxin, Met-SO formation, phosphorylation, or Lys acetylation, but we currently only understand the functional importance of a few of these PTMs. Some site modifications may represent molecular noise caused by spurious reactions. Third, different PTMs on the same protein or on different proteins in the same metabolic pathway can interact to fine-tune metabolic regulation. Fourth, PTMs take part in the repair of stress-induced damage (e.g., by reducing Met and Cys oxidation products) as well as adjusting metabolic functions in response to environmental variation, such as changes in light irradiance or oxygen availability. Finally, PTMs form a multidimensional regulatory system that provides the speed and flexibility needed for mitochondrial coordination far beyond that provided by changes in nuclear gene expression alone.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Plant cell
volume
32
issue
3
pages
22 pages
publisher
American Society of Plant Biologists
external identifiers
  • scopus:85081146333
  • pmid:31911454
ISSN
1040-4651
DOI
10.1105/tpc.19.00535
language
English
LU publication?
yes
id
56025bdc-d24f-4d9d-9f68-a72d0465ce8a
date added to LUP
2020-04-02 16:43:09
date last changed
2020-06-03 05:19:17
@article{56025bdc-d24f-4d9d-9f68-a72d0465ce8a,
  abstract     = {<p>Mitochondria function as hubs of plant metabolism. Oxidative phosphorylation produces ATP, but it is also a central high-capacity electron sink required by many metabolic pathways that must be flexibly coordinated and integrated. Here, we review the crucial roles of redox-associated posttranslational protein modifications (PTMs) in mitochondrial metabolic regulation. We discuss several major concepts. First, the major redox couples in the mitochondrial matrix (NAD, NADP, thioredoxin, glutathione, and ascorbate) are in kinetic steady state rather than thermodynamic equilibrium. Second, targeted proteomics have produced long lists of proteins potentially regulated by Cys oxidation/thioredoxin, Met-SO formation, phosphorylation, or Lys acetylation, but we currently only understand the functional importance of a few of these PTMs. Some site modifications may represent molecular noise caused by spurious reactions. Third, different PTMs on the same protein or on different proteins in the same metabolic pathway can interact to fine-tune metabolic regulation. Fourth, PTMs take part in the repair of stress-induced damage (e.g., by reducing Met and Cys oxidation products) as well as adjusting metabolic functions in response to environmental variation, such as changes in light irradiance or oxygen availability. Finally, PTMs form a multidimensional regulatory system that provides the speed and flexibility needed for mitochondrial coordination far beyond that provided by changes in nuclear gene expression alone.</p>},
  author       = {Møller, Ian Max and Igamberdiev, Abir U. and Bykova, Natalia V. and Finkemeier, Iris and Rasmusson, Allan G. and Schwarzländer, Markus},
  issn         = {1040-4651},
  language     = {eng},
  month        = {03},
  number       = {3},
  pages        = {573--594},
  publisher    = {American Society of Plant Biologists},
  series       = {The Plant cell},
  title        = {Matrix Redox Physiology Governs the Regulation of Plant Mitochondrial Metabolism through Posttranslational Protein Modifications},
  url          = {http://dx.doi.org/10.1105/tpc.19.00535},
  doi          = {10.1105/tpc.19.00535},
  volume       = {32},
  year         = {2020},
}