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Involvement of the N-terminal region and its characteristic coiled-coil fragment in the function and structure maintenance of E. coli LonA protease

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Abstract

The truncated form of E. coli LonA protease (EcLon) lacking the N-terminal fragment 1–172 (Lon173) and the variant with deleted coiled-coil (CC) fragment 173–283 (dCC-Lon, a deletion form) are produced and characterized to study the role of the N-terminal region in the functioning of this protease. A comparative analysis of the properties of full-length EcLon protease, dCC-Lon, and Lon173 as well as an earlier produced form with retained C-terminal region (235–280) of CC fragment, Lon235, is performed. As is shown, fragment 1–280 plays an important role in both formation of the ATPase site and maintenance of a stable EcLon protease conformation. Fragment 107–172 is of a paramount importance for implementation of the processive mechanism of ATP-dependent proteolysis.

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Abbreviations

AMPPNP:

adenosine 5′-(β,γ-imido)triphosphate

DTDP:

4,4′-dithiodipyridine

Nu:

nucleotide

PepTBE:

Suc-Phe-Leu-Phe-SBzl

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Authors and Affiliations

  1. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia

    A. G. Andrianova, A. M. Kudzhaev, E. S. Dubovtseva & T. V. Rotanova

Authors
  1. A. G. Andrianova
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  2. A. M. Kudzhaev
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  3. E. S. Dubovtseva
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  4. T. V. Rotanova
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Corresponding author

Correspondence to T. V. Rotanova.

Additional information

Original Russian Text © A.G. Andrianova, A.M. Kudzhaev, E.S. Dubovtseva, T.V. Rotanova, 2017, published in Bioorganicheskaya Khimiya, 2017, Vol. 43, No. 4, pp. 357–366.

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Andrianova, A.G., Kudzhaev, A.M., Dubovtseva, E.S. et al. Involvement of the N-terminal region and its characteristic coiled-coil fragment in the function and structure maintenance of E. coli LonA protease. Russ J Bioorg Chem 43, 368–376 (2017). https://doi.org/10.1134/S1068162017040021

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  • DOI: https://doi.org/10.1134/S1068162017040021

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