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@ARTICLE{Bovdilova:864225,
      author       = {Bovdilova, Anastasiia and Alexandre, Bruno M. and Höppner,
                      Astrid and Matias Luís, Inês and Alvarez, Clarisa E and
                      Bickel, David and Gohlke, Holger and Decker, Christina and
                      Nagel-Steger, Luitgard and Alseekh, Saleh and Fernie,
                      Alisdair R. and Drincovich, Maria F and Abreu, Isabel A. and
                      Maurino, Veronica G},
      title        = {{P}osttranslational modification of the {NADP}-malic enzyme
                      involved in {C}4 photosynthesis fine-tunes the enzymatic
                      activity during the day},
      journal      = {The plant cell},
      volume       = {31},
      number       = {10},
      issn         = {1040-4651},
      address      = {Rockville, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2019-04063},
      pages        = {2525-2539},
      year         = {2019},
      abstract     = {Evolution of the C4 photosynthetic pathway involved in some
                      cases recruitment of housekeeping proteins through gene
                      duplication and their further neofunctionalization.
                      NADP-malic enzyme (ME), the most widespread C4
                      decarboxylase, has increased its catalytic efficiency and
                      acquired regulatory properties that allowed it to
                      participate in the C4 pathway. Here, we show that regulation
                      of maize C4-NADP-ME activity is much more elaborated than
                      until now indicated. Using mass spectrometry, we identified
                      phosphorylation of the serine 419 (S419) of C4-NADP-ME in
                      protein extracts of maize leaves. The phosphorylation event
                      increases after the light turns on, with a peak at ZT2.
                      Phosphorylation of ZmC4-NADP-ME drastically decreases its
                      activity as shown by the low residual activity of the
                      recombinant phosphomimetic mutant. Analysis of the crystal
                      structure of C4-NADP-ME indicated that S419 is involved in
                      the binding of NADP at the active site. Molecular dynamics
                      simulations and effective binding energy computations
                      indicate a less favorable binding of the cofactor NADP in
                      the phosphomimetic and the phosphorylated variants. We
                      propose that phosphorylation of ZmC4-NADP-ME at S419 during
                      the first hours in the light is a cellular mechanism to
                      fine-tune the enzymatic activity to coordinate the carbon
                      concentration mechanism with the CO2 fixation rate, most
                      probably to avoid CO2 leakiness from bundle sheath cells.},
      cin          = {JSC / NIC / ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Forschergruppe Gohlke $(hkf7_20170501)$},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)hkf7_20170501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31363039},
      UT           = {WOS:000489162200022},
      doi          = {10.1105/tpc.19.00406},
      url          = {https://juser.fz-juelich.de/record/864225},
}