Abstract
Deletion of the transmembrane domain (TM-domain) of Archaeoglobus fulgidus LonB protease (Archaeoglobus fulgidus (AfLon)) was shown to result in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both α-helical and proteolytic domains (αP). The ΔTM-AfLon-S509A enzyme form, obtained by site-directed mutagenesis of the catalytic Ser residue, is capable of recombination with the αP fragment. The mixed oligomers were shown to be proteolytically active, which indicates a crucial role of subunit interactions in the activation of the AfLon proteolytic site. The thermophilic nature of AfLon protease was found to be due to the special features of the enzyme activity regulation, the structure of ATPase domain, and the quaternary structure.
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References
Neuwald, A.F., Aravind, L., Spouge, J.L., and Koonin, E.V., Genome Res., 1999, vol. 9, pp. 27–43.
Wickner, S., Maurizi, M.R., and Gottesman, S., Science, 1999, vol. 286, pp. 1888–1893.
Sauer, R.T., Bolon, D.N., Burton, B.M., Burton, R.E., Flynn, J.M., Grant, R.A., Hersch, G.L., Joshi, S.A., Kenniston, J.A., Levchenko, I., Neher, S.B., Oakes, E.S., Siddiqui, S.M., Wah, D.A., and Baker, T.A., Cell, 2004, vol. 119, pp. 9–18.
Rotanova, T.V., Melnikov, E.E., and Tsirulnikov, K.V., Bioorg. Khim., 2003, vol. 29, pp. 97–99; Rus. J. Bioorg. Chem., 2003, vol. 29, pp. 85–87.
Botos, I., Melnikov, E.E., Cherry, S., Tropea, J.E., Khalatova, A.G., Rasulova, F., Dauter, Z., Maurizi, M.R., Rotanova, T.V., Wlodawer, A., and Gustchina, A., J. Biol. Chem., 2004, vol. 279, pp. 8140–8148.
Botos, I., Melnikov, E.E., Cherry, S., Kozlov, S., Makhovskaya, O.V., Tropea, J.E., Gustchina, A., Rotanova, T.V., and Wlodawer, A., J. Mol. Biol., 2005, vol. 351, pp. 144–157.
Rotanova, T.V., Melnikov, E.E., Khalatova, A.G., Makhovskaya, O.V., Botos, I., Wlodawer, A., and Gustchina, A., Eur. J. Biochem., 2004, vol. 271, pp. 4865–4871.
Lupas, A.N. and Martin, J., Curr. Opin. Struct. Biol., 2002, vol. 12, pp. 746–753.
Iyer, L.M., Leipe, D.D., Koonin, E.V., and Aravind, L., J. Struct. Biol., 2004, vol. 146, pp. 11–31.
Goldberg, A.L., Moerschell, R.P., Chung, C.H., and Maurizi, M.R., Methods Enzymol., 1994, vol. 244, pp. 350–375.
Gottesman, S., Annu. Rev. Genet., 1996, vol. 30, pp. 465–506.
Makhovskaya, O.V., Mel’nikov, E.E., and Rotanova, T.V., Structural Organization and in vitro Functions of ATP-dependent LonB Proteinase from Arshaeoglobus fulgidus, Abstracts and Papers, Int. Conf. Contemporary Problems of Physiology and Biochemistry of Aquatic Organisms, Petrozavodsk, 2004, Nemova N.N., Ed. Petrozavodsk, 2005, pp. 131–138.
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Original Russian Text © O.V. Makhovskaya, S. Kozlov, I. Botos, A.A. Stepnov, A.G. Andrianova, A.E. Gushchina, A. Wlodawer, E.E. Mel’nikov, T.V. Rotanova, 2007, published in Bioorganicheskaya Khimiya, 2007, Vol. 33, No. 6, pp. 657–660.
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Makhovskaya, O.V., Kozlov, S., Botos, I. et al. Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: The contribution of the quaternary structure to the regulation of enzyme proteolytic activity. Russ J Bioorg Chem 33, 610–613 (2007). https://doi.org/10.1134/S1068162007060131
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DOI: https://doi.org/10.1134/S1068162007060131