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.
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.
Rotanova T.V. et al. Novel view of the architecture of the non-catalytic n-terminal region of ATP-dependent lona proteases // Biomeditsinskaya Khimiya. - 2010. - V. 56. -N 3. - P. 412-419.
Rotanova T.V. et al., "Novel view of the architecture of the non-catalytic n-terminal region of ATP-dependent lona proteases." Biomeditsinskaya Khimiya 56.3 (2010): 412-419.
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.
Rotanova T.V., Melnikov E.E., Khalatova A.G., Makhovskaya O.V., Botos I., Wlodawer A., Gustchina A. (2004) Eur. J. Biochem., 271, 4865-4871. CrossRef Scholar google search
Botos I., Melnikov E.E., Cherry S., Tropea J., Khalatova A.G., Rasulova F.S., Dauter Z., Maurizi M.R., Rotanova T.V., Wlodawer A., Gustchina A. (2004) J. Biol. Chem., 279, 8140-8148. CrossRef Scholar google search
Botos I., Melnikov E.E., Cherry S., Khalatova A.G., Rasulova F.S., Tropea J.E., Maurizi M.R., Rotanova T.V., Gustchina A., Wlodawer A. (2004) J. Struct. Biol., 146, 113-122. CrossRef Scholar google search
Li M., Rasulova F., Melnikov E.E., Rotanova T.V., Gustchina A., Maurizi M.R., Wlodawer A. (2005) Protein Sci., 14, 2895-2900. CrossRef Scholar google search
Botos I., Melnikov E.E., Cherry S., Kozlov S., Makhovskaya O.V., Tropea J., Gustchina A., Rotanova T.V., Wlodawer A. (2005) J. Mol. Biol., 351, 144-157. CrossRef Scholar google search
Im Y.J., Na Y., Kang G.B., Rho S.H., Kim M.K., Lee J.H., Chung C.H., Eom S.H. (2004) J. Biol. Chem. 279, 53451-53457. CrossRef Scholar google search
