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

   
Rotanova T.V.1 , Melnikov E.E.1

1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
Section: Short Communication
DOI: 10.18097/pbmc20105603412      PubMed Id: 20695221
Year: 2010  Volume: 56  Issue: 3  Pages: 412-419
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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Keywords: AAA+ proteins, ATP-dependent proteolysis, Lon protease, ClpB chaperones, propeller-like domain, coiled-coil region
Citation:

Rotanova, T. V., Melnikov, E. E. (2010). Novel view of the architecture of the non-catalytic n-terminal region of ATP-dependent lona proteases. Biomeditsinskaya khimiya, 56(3), 412-419.
This paper is also available as the English translation: 10.1134/S1990750810040141
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