ATP-dependent LonBA proteases of bacilli and clostridia
- Authors: Andrianova A.G.1, Kudzhaev A.M.1, Smirnov I.V.1, Rotanova T.V.1
-
Affiliations:
- Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
- Issue: Vol 50, No 5 (2024)
- Pages: 649-656
- Section: Articles
- URL: https://archivog.com/0132-3423/article/view/670802
- DOI: https://doi.org/10.31857/S0132342324050073
- EDN: https://elibrary.ru/LRAAQY
- ID: 670802
Cite item
Abstract
The Lon protease family belongs to the key peptide hydrolases of the protein quality control (PQC) system, which plays a leading role in maintaining the integrity of the cellular proteome in all natural kingdoms. Moreover, Lon proteases are the only family of ATP-dependent proteases of PQC which comprises a number of structurally distinct subfamilies. Recently, it has been suggested that the Lon family contains a previously unclassified LonBA subfamily, which includes enzymes from bacteria of the Bacilli and Clostridia classes. Using bioinformatics analysis, data were obtained on the structural features of enzymes of the putative new subfamily and on the existence of two different groups of Lon proteases in this subfamily.
Full Text

About the authors
A. G. Andrianova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Mikluho-Maklaya 16/10, Moscow, 117997
A. M. Kudzhaev
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Mikluho-Maklaya 16/10, Moscow, 117997
I. V. Smirnov
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Mikluho-Maklaya 16/10, Moscow, 117997
T. V. Rotanova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
Author for correspondence.
Email: tatyana.rotanova@ibch.ru
Russian Federation, ul. Mikluho-Maklaya 16/10, Moscow, 117997
References
- Kudzhaev A.M., Andrianova A.G., Gustchina A.E., Smirnov I.V., Rotanova T.V. // Russ. J. Bioorg. Chem. 2022. V. 48. P. 678–709. https://doi.org/10.1134/s1068162022040136
- Gustchina A., Li M., Andrianova A.G., Kudzhaev A.M., Lountos G.T., Sekula B., Cherry S., Tropea J.E., Smirnov I.V., Wlodawer A., Rotanova T.V. // Int. J. Mol. Sci. 2022. V. 23. P. 11425. https://doi.org/10.3390/ijms231911425
- Wlodawer A., Sekula B., Gustchina A., Rotanova T.V. // J. Mol. Biol. 2022. V. 434. P. 167504. https://doi.org/10.1016/j.jmb.2022.167504
- Liao J.H., Kuo C.I., Huang Y.Y., Lin Y.C., Lin Y.C., Yang C.Y., Wu W.L., Chang W.H., Liaw Y.C., Lin L.H., Chang C.I., Wu S.H. // PLoS One. 2012. V. 7. P. e40226. https://doi.org/10.1371/journal.pone.0040226
- Sauer R.T., Baker T.A. // Ann. Rev. Biochem. 2011. V. 80. P. 587–612. https://doi.org/10.1146/annurev-biochem-060408-172623
- Rawlings N.D., Barrett A.J., Thomas P.D., Huang X., Bateman A., Finn R.D. // Nucleic Acids Res. 2018. V. 46. P. 624–632. https://doi.org/10.1093/nar/gkx1134
- Gottesman S. // Annu. Rev. Cell Dev. Biol. 2003. V. 19. P. 565–587. https://doi.org/10.1146/annurev.cellbio.19.110701.153228
- Pei J., Yan J., Jiang Y. // Hindawi Publishing Corporation. Archaea. 2016. Article ID 5759765. https://doi.org/10.1155/2016/5759765
- Cerletti M., Paggi R.A., Guevara C.R., Poetsch A., De Castro R.E. // J. Proteomics. 2015. V. 121. P. 1–14. https://doi.org/10.1016/j.jprot.2015.03.016
- Maehara T., Hoshino T., Nakamura A. // Extremophiles. 2008. V. 12. P. 285–296. https://doi.org/10.1007/s00792-007-0129-3
- Rotanova T.V., Melnikov E.E., Tsirulnikov K.B. // Russ. J. Bioorg. Chem. 2003. V. 29. P. 85–87.
- Rotanova T.V., Melnikov E.E., Khalatova A.G., Makhovskaya O.V., Botos I., Wlodawer A., Gustchina A. // Eur. J. Biochem. 2004. V. 271. P. 4865–4871. https://doi.org/10.1111/j.1432-1033.2004.04452.x
- Rotanova T.V., Botos I., Melnikov E.E., Rasulova F., Gustchina A., Maurizi M.R., Wlodawer A. // Protein Sci. 2006. V. 15. P. 1815–1828. https://doi.org/10.1110/ps.052069306
- Iyer L.M., Leipe D.D., Koonin E.V., Aravind L. // J. Struct. Biol. 2004. V. 146. P. 11–31. https://doi.org/10.1016/j.jsb.2003.10.010
- Lupas A.N., Martin J. // Curr. Opin. Struct. Biol. 2002. V. 12. P. 746–753. https://doi.org/10.1016/s0959-440x(02)00388-3
- Bittner L.M., Arends J., Narberhaus F. // Biopolymers. 2016. V. 105. P. 505–517. https://doi.org/10.1002/bip.22831
- Liao J.H., Ihara K., Kuo C.I., Huang K.F., Wakatsuki S., Wu S.H., Chang C.I. // Acta Cryst. 2013. V. 69. P. 1395–1402. https://doi.org/10.1107/S0907444913008214
- Rotanova T.V., Andrianova A.G., Kudzhaev A.M., Li M., Botos I., Wlodawer A., Gustchina A. // FEBS Open Bio. 2019. V. 9. P. 1536–1551. https://doi.org/10.1002/2211-5463.12691
Supplementary files
