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The mitochondrial external NADPH dehydrogenase modulates the leaf NADPH/NADP+ ratio in transgenic Nicotiana sylvestris

Liu, Yunjun LU ; Norberg, Fredrik EB ; Szilagyi, Anna LU ; De Paepe, Rosine ; Åkerlund, Hans-Erik LU and Rasmusson, Allan LU (2008) In Plant and Cell Physiology 49(1). p.251-263
Abstract
Plant mitochondria contain alternative external NAD(P)H dehydrogenases, which oxidise cytosolic NADH or NADPH and reduce ubiquinone without inherent linkage to proton pumping and ATP production. In potato, St-NDB1 is an external Ca2+-dependent NADPH dehydrogenase. The physiological function of this enzyme was investigated in homozygous Nicotiana sylvestris lines overexpressing St-ndb1 and co-suppressing St-ndb1 and an N. sylvestris ndb1. In leaf mitochondria isolated from the overexpressor lines, higher activity of alternative oxidase (AOX) was detected. However, the AOX induction was substantially weaker than in the complex I deficient CMSII mutant, previously shown to contain elevated amounts of NAD(P)H dehydrogenases and AOX. An aox1b... (More)
Plant mitochondria contain alternative external NAD(P)H dehydrogenases, which oxidise cytosolic NADH or NADPH and reduce ubiquinone without inherent linkage to proton pumping and ATP production. In potato, St-NDB1 is an external Ca2+-dependent NADPH dehydrogenase. The physiological function of this enzyme was investigated in homozygous Nicotiana sylvestris lines overexpressing St-ndb1 and co-suppressing St-ndb1 and an N. sylvestris ndb1. In leaf mitochondria isolated from the overexpressor lines, higher activity of alternative oxidase (AOX) was detected. However, the AOX induction was substantially weaker than in the complex I deficient CMSII mutant, previously shown to contain elevated amounts of NAD(P)H dehydrogenases and AOX. An aox1b and an aox2 gene were up-regulated in CMSII, but only aox1b showed a response, albeit smaller, in the transgenic lines, indicating differences in AOX activation between the genotypes. As in CMSII, the increase of AOX in the overexpressing lines was not due to a general oxidative stress. The lines overexpressing St-ndb1 had consistently lowered leaf NADPH/NADP+ ratios in the light and variably decreased levels in darkness, but unchanged NADH/NAD+ ratios. CMSII instead had similar NADPH/NADP+ and lower NADH/NAD+ ratios than wildtype. These results demonstrate that St-NDB1 is able to modulate the cellular balance of NADPH and NADP+ at least in the day and that reduction of NADP(H) and NAD(H) is independently controlled. Similar growth rates, chloroplast malate dehydrogenase activation and xanthophyll ratios indicate that the change in reduction does not communicate to the chloroplast, and that the cell tolerates significant changes in NADP(H) reduction without deleterious effects. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Alternative oxidase - Chloroplast - Electron transport chain - NADPH - Mitochondria - Transgenic plants
in
Plant and Cell Physiology
volume
49
issue
1
pages
251 - 263
publisher
Oxford University Press
external identifiers
  • wos:000253021400011
  • scopus:38949092105
ISSN
1471-9053
DOI
10.1093/pcp/pcn001
language
English
LU publication?
yes
id
4be93f74-725e-4e63-bfa7-2fc4e69dd229 (old id 941906)
date added to LUP
2016-04-01 12:05:40
date last changed
2024-01-08 08:10:54
@article{4be93f74-725e-4e63-bfa7-2fc4e69dd229,
  abstract     = {{Plant mitochondria contain alternative external NAD(P)H dehydrogenases, which oxidise cytosolic NADH or NADPH and reduce ubiquinone without inherent linkage to proton pumping and ATP production. In potato, St-NDB1 is an external Ca2+-dependent NADPH dehydrogenase. The physiological function of this enzyme was investigated in homozygous Nicotiana sylvestris lines overexpressing St-ndb1 and co-suppressing St-ndb1 and an N. sylvestris ndb1. In leaf mitochondria isolated from the overexpressor lines, higher activity of alternative oxidase (AOX) was detected. However, the AOX induction was substantially weaker than in the complex I deficient CMSII mutant, previously shown to contain elevated amounts of NAD(P)H dehydrogenases and AOX. An aox1b and an aox2 gene were up-regulated in CMSII, but only aox1b showed a response, albeit smaller, in the transgenic lines, indicating differences in AOX activation between the genotypes. As in CMSII, the increase of AOX in the overexpressing lines was not due to a general oxidative stress. The lines overexpressing St-ndb1 had consistently lowered leaf NADPH/NADP+ ratios in the light and variably decreased levels in darkness, but unchanged NADH/NAD+ ratios. CMSII instead had similar NADPH/NADP+ and lower NADH/NAD+ ratios than wildtype. These results demonstrate that St-NDB1 is able to modulate the cellular balance of NADPH and NADP+ at least in the day and that reduction of NADP(H) and NAD(H) is independently controlled. Similar growth rates, chloroplast malate dehydrogenase activation and xanthophyll ratios indicate that the change in reduction does not communicate to the chloroplast, and that the cell tolerates significant changes in NADP(H) reduction without deleterious effects.}},
  author       = {{Liu, Yunjun and Norberg, Fredrik EB and Szilagyi, Anna and De Paepe, Rosine and Åkerlund, Hans-Erik and Rasmusson, Allan}},
  issn         = {{1471-9053}},
  keywords     = {{Alternative oxidase - Chloroplast - Electron transport chain - NADPH - Mitochondria - Transgenic plants}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{251--263}},
  publisher    = {{Oxford University Press}},
  series       = {{Plant and Cell Physiology}},
  title        = {{The mitochondrial external NADPH dehydrogenase modulates the leaf NADPH/NADP+ ratio in transgenic Nicotiana sylvestris}},
  url          = {{http://dx.doi.org/10.1093/pcp/pcn001}},
  doi          = {{10.1093/pcp/pcn001}},
  volume       = {{49}},
  year         = {{2008}},
}