4.7 Article

Arabidopsis tic62 trol Mutant Lacking Thylakoid-Bound FerredoxinNADP Oxidoreductase Shows Distinct Metabolic Phenotype

期刊

MOLECULAR PLANT
卷 7, 期 1, 页码 45-57

出版社

OXFORD UNIV PRESS
DOI: 10.1093/mp/sst129

关键词

carbon assimilation; ferredoxinNADP oxidoreductase; photosynthesis; chloroplast; stromal metabolism; Tic62; TROL

资金

  1. Academy of Finland [263667, 118637, 256784]
  2. Deutsche Forschungsgemeinschaft [Ge 878/5-1, Ge 878/8-1, SFB 594, IRTG 1525-1, EXC 1028]
  3. Munich Center for Integrated Protein Science CiPSM
  4. National Science Foundation

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Ferredoxin-NADP(+) oxidoreductase (FNR), functioning in the last step of the photosynthetic electron transfer chain, exists both as a soluble protein in the chloroplast stroma and tightly attached to chloroplast membranes. Surface plasmon resonance assays showed that the two FNR isoforms, LFNR1 and LFNR2, are bound to the thylakoid membrane via the C-terminal domains of Tic62 and TROL proteins in a pH-dependent manner. The tic62 trol double mutants contained a reduced level of FNR, exclusively found in the soluble stroma. Although the mutant plants showed no visual phenotype or defects in the function of photosystems under any conditions studied, a low ratio of NADPH/NADP(+) was detected. Since the CO2 fixation capacity did not differ between the tic62 trol plants and wild-type, it seems that the plants are able to funnel reducing power to most crucial reactions to ensure survival and fitness of the plants. However, the activity of malate dehydrogenase was down-regulated in the mutant plants. Apparently, the plastid metabolism is able to cope with substantial changes in directing the electrons from the light reactions to stromal metabolism and thus only few differences are visible in steady-state metabolite pool sizes of the tic62 trol plants.

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