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@ARTICLE{Krishnamurthy:943337,
      author       = {Krishnamurthy, Srinath and Sardis, Marios-Frantzeskos and
                      Eleftheriadis, Nikolaos and Chatzi, Katerina E. and Smit,
                      Jochem H. and Karathanou, Konstantina and Gouridis, Giorgos
                      and Portaliou, Athina G. and Bondar, Ana-Nicoleta and
                      Karamanou, Spyridoula and Economou, Anastassios},
      title        = {{P}reproteins couple the intrinsic dynamics of {S}ec{A} to
                      its {ATP}ase cycle to translocate via a catch and release
                      mechanism},
      journal      = {Cell reports},
      volume       = {38},
      number       = {6},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2023-00943},
      pages        = {110346 -},
      year         = {2022},
      abstract     = {Protein machines undergo conformational motions to interact
                      with and manipulate polymeric substrates. The Sec
                      translocase promiscuously recognizes, becomes activated, and
                      secretes >500 non-folded preprotein clients across bacterial
                      cytoplasmic membranes. Here, we reveal that the intrinsic
                      dynamics of the translocase ATPase, SecA, and of preproteins
                      combine to achieve translocation. SecA possesses an
                      intrinsically dynamic preprotein clamp attached to an
                      equally dynamic ATPase motor. Alternating motor
                      conformations are finely controlled by the γ-phosphate of
                      ATP, while ADP causes motor stalling, independently of clamp
                      motions. Functional preproteins physically bridge these
                      independent dynamics. Their signal peptides promote clamp
                      closing; their mature domain overcomes the rate-limiting ADP
                      release. While repeated ATP cycles shift the motor between
                      unique states, multiple conformationally frustrated prongs
                      in the clamp repeatedly “catch and release” trapped
                      preprotein segments until translocation completion. This
                      universal mechanism allows any preprotein to promiscuously
                      recognize the translocase, usurp its intrinsic dynamics, and
                      become secreted.},
      cin          = {IAS-5 / INM-9},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35139375},
      UT           = {WOS:000754407500004},
      doi          = {10.1016/j.celrep.2022.110346},
      url          = {https://juser.fz-juelich.de/record/943337},
}