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@ARTICLE{Mielke:890970,
      author       = {Mielke, Kati and Wagner, Raik and Mishra, Laxmi S and
                      Demir, Fatih and Perrar, Andreas and Huesgen, Pitter F and
                      Funk, Christiane},
      title        = {{A}bundance of metalloprotease {F}ts{H}12 modulates
                      chloroplast development in {A}rabidopsis thaliana},
      journal      = {The journal of experimental botany},
      volume       = {72},
      number       = {9},
      issn         = {1460-2431},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2021-01286},
      pages        = {3455–3473},
      year         = {2021},
      abstract     = {The ATP-dependent metalloprotease FtsH12 (filamentation
                      temperature sensitive protein H 12) has been suggested to
                      participate in a heteromeric motor complex, driving protein
                      translocation into the chloroplast. FtsH12 was
                      immuno-detected in proplastids, seedlings, leaves, and
                      roots. Expression of Myc-tagged FtsH12 under its native
                      promotor allowed identification of FtsHi1, 2, 4, and 5, and
                      plastidic NAD-malate dehydrogenase, five of the six
                      interaction partners in the suggested import motor complex.
                      Arabidopsis thaliana mutant seedlings with reduced FTSH12
                      abundance exhibited pale cotyledons and small, deformed
                      chloroplasts with altered thylakoid structure. Mature plants
                      retained these chloroplast defects, resulting in slightly
                      variegated leaves and lower chlorophyll content. Label-free
                      proteomics revealed strong changes in the proteome
                      composition of FTSH12 knock-down seedlings, reflecting
                      impaired plastid development. The composition of the
                      translocon on the inner chloroplast membrane (TIC) protein
                      import complex was altered, with coordinated reduction of
                      the FtsH12-FtsHi complex subunits and accumulation of the 1
                      MDa TIC complex subunits TIC56, TIC214 and TIC22-III. FTSH12
                      overexpressor lines showed no obvious phenotype, but still
                      displayed distinct differences in their proteome.
                      N-terminome analyses further demonstrated normal proteolytic
                      maturation of plastid-imported proteins irrespective of
                      FTSH12 abundance. Together, our data suggest that FtsH12 has
                      highest impact during seedling development; its abundance
                      alters the plastid import machinery and impairs chloroplast
                      development.},
      cin          = {ZEA-3},
      ddc          = {580},
      cid          = {I:(DE-Juel1)ZEA-3-20090406},
      pnm          = {217 - Für eine nachhaltige Bio-Ökonomie – von
                      Ressourcen zu Produkten (POF4-217) / ProPlantStress -
                      Proteolytic processing in plant stress signal transduction
                      and responses to abiotic stress and pathogen attack
                      (639905)},
      pid          = {G:(DE-HGF)POF4-217 / G:(EU-Grant)639905},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33216923},
      UT           = {WOS:000707097500010},
      doi          = {10.1093/jxb/eraa550},
      url          = {https://juser.fz-juelich.de/record/890970},
}