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@ARTICLE{Hdig:902470,
      author       = {Hüdig, Meike and Tronconi, Marcos A and Zubimendi, Juan P
                      and Sage, Tammy L and Poschmann, Gereon and Bickel, David
                      and Gohlke, Holger and Maurino, Veronica G},
      title        = {{R}espiratory and {C}4-photosynthetic {NAD}-malic enzyme
                      coexist in bundle sheath cell mitochondria and evolved via
                      association of differentially adapted subunits},
      journal      = {The plant cell},
      volume       = {34},
      number       = {1},
      issn         = {1040-4651},
      address      = {Rockville, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2021-04289},
      pages        = {597–615},
      year         = {2022},
      abstract     = {In plant mitochondria, nicotinamide adenine dinucleotide
                      phosphate (NAD)-malic enzyme (NAD-ME) has a housekeeping
                      function in malate respiration. In different plant lineages,
                      NAD-ME was independently co-opted in C4 photosynthesis. In
                      the C4 Cleome species Gynandropsis gynandra and Cleome
                      angustifolia, all NAD-ME genes (NAD-MEα, NAD-MEβ1, and
                      NAD-MEβ2) were affected by C4 evolution and are expressed
                      at higher levels than their orthologs in the C3 species
                      Tarenaya hassleriana. In Tarenaya hassleriana, the NAD-ME
                      housekeeping function is performed by two heteromers,
                      NAD-MEα/β1 and NAD-MEα/β2, with similar biochemical
                      properties. In both C4 species, this role is restricted to
                      NAD-MEα/β2. In the C4 species, NAD-MEα/β1 is exclusively
                      present in the leaves, where it accounts for most of the
                      enzymatic activity. GgNAD-MEα/β1 exhibits high catalytic
                      efficiency and is differentially activated by the C4
                      intermediate aspartate, confirming its role as the
                      C4-decarboxylase. During C4 evolution, NAD-MEβ1 lost its
                      catalytic activity; its contribution to the enzymatic
                      activity results from a stabilizing effect on the associated
                      α-subunit and the adquisition of regulatory properties. We
                      conclude that in bundle sheath cell mitochondria of C4
                      species, the functions of NAD-ME as C4 photosynthetic
                      decarboxylase and as a housekeeping enzyme coexist and are
                      performed by isoforms that combine the same α subunit with
                      differentially adapted β subunits.},
      cin          = {IBG-4 / JSC / NIC / IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)IBI-7-20200312},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217) / 2172 - Utilization of renewable
                      carbon and energy sources and engineering of ecosystem
                      functions (POF4-217) / 5111 - Domain-Specific Simulation
                      $\&$ Data Life Cycle Labs (SDLs) and Research Groups
                      (POF4-511) / Forschergruppe Gohlke $(hkf7_20200501)$ / 5241
                      - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-2171 / G:(DE-HGF)POF4-2172 /
                      G:(DE-HGF)POF4-5111 / $G:(DE-Juel1)hkf7_20200501$ /
                      G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34734993},
      UT           = {WOS:000745840600036},
      doi          = {10.1093/plcell/koab265},
      url          = {https://juser.fz-juelich.de/record/902470},
}