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Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases

ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS database to three subfamilies (A, B, and C). All Lons are...

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Autores principales: Gustchina, Alla, Li, Mi, Andrianova, Anna G., Kudzhaev, Arsen M., Lountos, George T., Sekula, Bartosz, Cherry, Scott, Tropea, Joseph E., Smirnov, Ivan V., Wlodawer, Alexander, Rotanova, Tatyana V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9569914/
https://www.ncbi.nlm.nih.gov/pubmed/36232729
http://dx.doi.org/10.3390/ijms231911425
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author Gustchina, Alla
Li, Mi
Andrianova, Anna G.
Kudzhaev, Arsen M.
Lountos, George T.
Sekula, Bartosz
Cherry, Scott
Tropea, Joseph E.
Smirnov, Ivan V.
Wlodawer, Alexander
Rotanova, Tatyana V.
author_facet Gustchina, Alla
Li, Mi
Andrianova, Anna G.
Kudzhaev, Arsen M.
Lountos, George T.
Sekula, Bartosz
Cherry, Scott
Tropea, Joseph E.
Smirnov, Ivan V.
Wlodawer, Alexander
Rotanova, Tatyana V.
author_sort Gustchina, Alla
collection PubMed
description ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS database to three subfamilies (A, B, and C). All Lons are single-chain, multidomain proteins containing an ATPase and protease domains, with different additional elements present in each subfamily. LonA and LonC proteases are soluble cytoplasmic enzymes, whereas LonBs are membrane-bound. Based on an analysis of the available sequences of Lon proteases, we identified a number of enzymes currently assigned to the LonB subfamily that, although presumably membrane-bound, include structural features more similar to their counterparts in the LonA subfamily. This observation was confirmed by the crystal structure of the proteolytic domain of the enzyme previously assigned as Bacillus subtilis LonB, combined with the modeled structure of its ATPase domain. Several structural features present in both domains differ from their counterparts in either LonA or LonB subfamilies. We thus postulate that this enzyme is the founding member of a newly identified LonBA subfamily, so far found only in the gene sequences of firmicutes.
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spelling pubmed-95699142022-10-17 Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases Gustchina, Alla Li, Mi Andrianova, Anna G. Kudzhaev, Arsen M. Lountos, George T. Sekula, Bartosz Cherry, Scott Tropea, Joseph E. Smirnov, Ivan V. Wlodawer, Alexander Rotanova, Tatyana V. Int J Mol Sci Article ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS database to three subfamilies (A, B, and C). All Lons are single-chain, multidomain proteins containing an ATPase and protease domains, with different additional elements present in each subfamily. LonA and LonC proteases are soluble cytoplasmic enzymes, whereas LonBs are membrane-bound. Based on an analysis of the available sequences of Lon proteases, we identified a number of enzymes currently assigned to the LonB subfamily that, although presumably membrane-bound, include structural features more similar to their counterparts in the LonA subfamily. This observation was confirmed by the crystal structure of the proteolytic domain of the enzyme previously assigned as Bacillus subtilis LonB, combined with the modeled structure of its ATPase domain. Several structural features present in both domains differ from their counterparts in either LonA or LonB subfamilies. We thus postulate that this enzyme is the founding member of a newly identified LonBA subfamily, so far found only in the gene sequences of firmicutes. MDPI 2022-09-28 /pmc/articles/PMC9569914/ /pubmed/36232729 http://dx.doi.org/10.3390/ijms231911425 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Gustchina, Alla
Li, Mi
Andrianova, Anna G.
Kudzhaev, Arsen M.
Lountos, George T.
Sekula, Bartosz
Cherry, Scott
Tropea, Joseph E.
Smirnov, Ivan V.
Wlodawer, Alexander
Rotanova, Tatyana V.
Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
title Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
title_full Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
title_fullStr Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
title_full_unstemmed Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
title_short Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
title_sort unique structural fold of lonba protease from bacillus subtilis, a member of a newly identified subfamily of lon proteases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9569914/
https://www.ncbi.nlm.nih.gov/pubmed/36232729
http://dx.doi.org/10.3390/ijms231911425
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