Novel view of the architecture of the non-catalytic n-terminal region of ATP-dependent lona proteases

   


1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
Type: Short communication
DOI: 10.18097/pbmc20105603412      UDK: 577.152.342*1'134; 577.322.23      PubMed Id: 20695221
Year: 2010 vol: 56  issue:3  pages: 412-419
Abstract: ATP-Dependent Lon proteases are components of the protein quality control system, which maintains a keeping of cellular proteome. Lon family consists of two subfamilies A and B, differing in subunit architecture and intracellular location. The reinterpretation of the domain organization of the non-catalytic N-terminal region of ATP-dependent LonA proteases is proposed. Using Escherichia coli LonA protease (EcLon) as an example it has been shown that a fragment (αN-domain), which is located between the N-terminal domain and the ААА+ module of that protein, is similar to the α1-domain of the first ААА+ module of chaperone-disaggregase ClpB. A coiled-coil (СС) region included in the αN-domain of LonA is similar to the M domain of ClpB chaperones, which is inserted into the α1-domain. This region is suggested to adopt the structure similar to the propeller-like (PL) domain. The typical architecture of the N-terminal region of LonA proteases is postulated to be characterized by the obligatory presence of a PL domain, included in the αN-domain, but may vary in the length and topology of the preceding N-terminal domain.
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Reference: Rotanova T.V., Melnikov E.E., Novel view of the architecture of the non-catalytic n-terminal region of ATP-dependent lona proteases, Biomeditsinskaya khimiya, 2010, vol: 56(3), 412-419.
This paper is also available as the English translation:10.1134/S1990750810040141
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