Unique Structural Organization of ATP-Dependent LonA
Proteases

T. V. Rotanova^a,1, N. I. Dergousova^a, A. D. Morozkin^b

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

^b Russian Cardiology Research and Production Center, Institute of Experimental Cardiology,
Cherepkovskaya ul. 15a, Moscow, 121552 Russia

Received November 29, 2012; in final form, December 6, 2012

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 -helical domain including a coiled-coil region, which is similar to the -helical domain
of the AAA⁺-1 module of the chaperone-disagregases ClpB/Hsp104.

Keywords: AAA⁺ proteins, ATP-dependent proteolysis, LonA proteases, ClpB chaperones, primary and second-
ary structure, domain organization, coiled-coil region

DOI: 10.1134/S1068162013030114

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