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Unique structural organization of ATP-dependent LonA proteases

Abstract

Homooligomeric LonA proteases are the key components of the protein quality control system in bacteria and eukaryotes. Domain organization of the common pool of LonA proteases is determined by the comparative analysis of primary and secondary structures of a number of bacterial and eukaryotic enzymes. The similarity of individual enzyme domains was estimated, domain-domain linker areas were revealed, and regions that are capable of including intercalated peptide fragments were identified. LonA proteases were shown to be unique AAA+ proteins, because in addition to the classic AAA+ module they contain a part of another AAA+ module, namely the α-helical domain including a coiled-coil region, which is similar to the α-helical domain of the AAA+-1 module of the chaperone-disagregases ClpB/Hsp104.

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Correspondence to T. V. Rotanova.

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Original Russian Text © T.V. Rotanova, N.I. Dergousova, A.D. Morozkin, 2013, published in Bioorganicheskaya Khimiya, 2013, Vol. 39, No. 3, pp. 303–319.

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Rotanova, T.V., Dergousova, N.I. & Morozkin, A.D. Unique structural organization of ATP-dependent LonA proteases. Russ J Bioorg Chem 39, 268–282 (2013). https://doi.org/10.1134/S1068162013030114

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  • DOI: https://doi.org/10.1134/S1068162013030114

Keywords

  • AAA+ proteins
  • ATP-dependent proteolysis
  • LonA proteases
  • ClpB chaperones
  • primary and secondary structure
  • domain organization
  • coiled-coil region