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@ARTICLE{Remes:1007362,
      author       = {Remes, Cristina and Khawaja, Anas and Pearce, Sarah F and
                      Dinan, Adam M and Gopalakrishna, Shreekara and Cipullo,
                      Miriam and Kyriakidis, Vasileios and Zhang, Jingdian and
                      Dopico, Xaquin Castro and Yukhnovets, Olessya and Atanassov,
                      Ilian and Firth, Andrew E and Cooperman, Barry and Rorbach,
                      Joanna},
      title        = {{T}ranslation initiation of leaderless and polycistronic
                      transcripts in mammalian mitochondria},
      journal      = {Nucleic acids research},
      volume       = {51},
      number       = {2},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2023-02031},
      pages        = {891 - 907},
      year         = {2023},
      abstract     = {The synthesis of mitochondrial OXPHOS complexes is central
                      to cellular metabolism, yet many molecular details of
                      mitochondrial translation remain elusive. It has been
                      commonly held view that translation initiation in human
                      mitochondria proceeded in a manner similar to bacterial
                      systems, with the mitoribosomal small subunit bound to the
                      initiation factors, mtIF2 and mtIF3, along with initiator
                      tRNA and an mRNA. However, unlike in bacteria, most human
                      mitochondrial mRNAs lack 5′ leader sequences that can
                      mediate small subunit binding, raising the question of how
                      leaderless mRNAs are recognized by mitoribosomes. By using
                      novel in vitro mitochondrial translation initiation assays,
                      alongside biochemical and genetic characterization of
                      cellular knockouts of mitochondrial translation factors, we
                      describe unique features of translation initiation in human
                      mitochondria. We show that in vitro, leaderless mRNA
                      transcripts can be loaded directly onto assembled 55S
                      mitoribosomes, but not onto the mitoribosomal small subunit
                      (28S), in a manner that requires initiator fMet-tRNAMet
                      binding. In addition, we demonstrate that in human cells and
                      in vitro, mtIF3 activity is not required for translation of
                      leaderless mitochondrial transcripts but is essential for
                      translation of ATP6 in the case of the bicistronic ATP8/ATP6
                      transcript. Furthermore, we show that mtIF2 is indispensable
                      for mitochondrial protein synthesis. Our results demonstrate
                      an important evolutionary divergence of the mitochondrial
                      translation system and further our fundamental understanding
                      of a process central to eukaryotic metabolism.},
      cin          = {IBI-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-6-20200312},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535)},
      pid          = {G:(DE-HGF)POF4-5352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36629253},
      UT           = {WOS:000910085600001},
      doi          = {10.1093/nar/gkac1233},
      url          = {https://juser.fz-juelich.de/record/1007362},
}