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Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA

Serratia proteamaculans synthesizes the intracellular metalloprotease protealysin. This work was aimed at searching for bacterial substrates of protealysin among the proteins responsible for replication and cell division. We have shown that protealysin unlimitedly cleaves the SOS response protein Re...

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Autores principales: Tsaplina, Olga, Khaitlina, Sofia, Chukhontseva, Ksenia, Karaseva, Maria, Demidyuk, Ilya, Bakhlanova, Irina, Baitin, Dmitry, Artamonova, Tatiana, Vedyaykin, Alexey, Khodorkovskii, Mikhail, Vishnyakov, Innokentii
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505478/
https://www.ncbi.nlm.nih.gov/pubmed/36142700
http://dx.doi.org/10.3390/ijms231810787
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author Tsaplina, Olga
Khaitlina, Sofia
Chukhontseva, Ksenia
Karaseva, Maria
Demidyuk, Ilya
Bakhlanova, Irina
Baitin, Dmitry
Artamonova, Tatiana
Vedyaykin, Alexey
Khodorkovskii, Mikhail
Vishnyakov, Innokentii
author_facet Tsaplina, Olga
Khaitlina, Sofia
Chukhontseva, Ksenia
Karaseva, Maria
Demidyuk, Ilya
Bakhlanova, Irina
Baitin, Dmitry
Artamonova, Tatiana
Vedyaykin, Alexey
Khodorkovskii, Mikhail
Vishnyakov, Innokentii
author_sort Tsaplina, Olga
collection PubMed
description Serratia proteamaculans synthesizes the intracellular metalloprotease protealysin. This work was aimed at searching for bacterial substrates of protealysin among the proteins responsible for replication and cell division. We have shown that protealysin unlimitedly cleaves the SOS response protein RecA. Even 20% of the cleaved RecA in solution appears to be incorporated into the polymer of uncleaved monomers, preventing further polymerization and inhibiting RecA ATPase activity. Transformation of Escherichia coli with a plasmid carrying the protealysin gene reduces the bacterial UV survival up to 10 times. In addition, the protealysin substrate is the FtsZ division protein, found in both E. coli and Acholeplasma laidlawii, which is only 51% identical to E. coli FtsZ. Protealysin cleaves FtsZ at the linker between the globular filament-forming domain and the C-terminal peptide that binds proteins on the bacterial membrane. Thus, cleavage of the C-terminal segment by protealysin can lead to the disruption of FtsZ’s attachment to the membrane, and thereby inhibit bacterial division. Since the protealysin operon encodes not only the protease, but also its inhibitor, which is typical for the system of interbacterial competition, we assume that in the case of penetration of protealysin into neighboring bacteria that do not synthesize a protealysin inhibitor, cleavage of FtsZ and RecA by protealysin may give S. proteamaculans an advantage in interbacterial competition.
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spelling pubmed-95054782022-09-24 Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA Tsaplina, Olga Khaitlina, Sofia Chukhontseva, Ksenia Karaseva, Maria Demidyuk, Ilya Bakhlanova, Irina Baitin, Dmitry Artamonova, Tatiana Vedyaykin, Alexey Khodorkovskii, Mikhail Vishnyakov, Innokentii Int J Mol Sci Article Serratia proteamaculans synthesizes the intracellular metalloprotease protealysin. This work was aimed at searching for bacterial substrates of protealysin among the proteins responsible for replication and cell division. We have shown that protealysin unlimitedly cleaves the SOS response protein RecA. Even 20% of the cleaved RecA in solution appears to be incorporated into the polymer of uncleaved monomers, preventing further polymerization and inhibiting RecA ATPase activity. Transformation of Escherichia coli with a plasmid carrying the protealysin gene reduces the bacterial UV survival up to 10 times. In addition, the protealysin substrate is the FtsZ division protein, found in both E. coli and Acholeplasma laidlawii, which is only 51% identical to E. coli FtsZ. Protealysin cleaves FtsZ at the linker between the globular filament-forming domain and the C-terminal peptide that binds proteins on the bacterial membrane. Thus, cleavage of the C-terminal segment by protealysin can lead to the disruption of FtsZ’s attachment to the membrane, and thereby inhibit bacterial division. Since the protealysin operon encodes not only the protease, but also its inhibitor, which is typical for the system of interbacterial competition, we assume that in the case of penetration of protealysin into neighboring bacteria that do not synthesize a protealysin inhibitor, cleavage of FtsZ and RecA by protealysin may give S. proteamaculans an advantage in interbacterial competition. MDPI 2022-09-15 /pmc/articles/PMC9505478/ /pubmed/36142700 http://dx.doi.org/10.3390/ijms231810787 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
Tsaplina, Olga
Khaitlina, Sofia
Chukhontseva, Ksenia
Karaseva, Maria
Demidyuk, Ilya
Bakhlanova, Irina
Baitin, Dmitry
Artamonova, Tatiana
Vedyaykin, Alexey
Khodorkovskii, Mikhail
Vishnyakov, Innokentii
Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA
title Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA
title_full Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA
title_fullStr Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA
title_full_unstemmed Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA
title_short Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA
title_sort protealysin targets the bacterial housekeeping proteins ftsz and reca
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505478/
https://www.ncbi.nlm.nih.gov/pubmed/36142700
http://dx.doi.org/10.3390/ijms231810787
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