Version 1
: Received: 24 May 2024 / Approved: 27 May 2024 / Online: 27 May 2024 (13:55:36 CEST)
How to cite:
Al Ebrahim, R. N.; Alekseeva, M. G.; Bazhenov, S. V.; Fomin, V. V.; Mavletova, D. A.; Nesterov, A. A.; Poluektova, E. U.; Danilenko, V. N.; Manukhov, I. V. ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus fermentum U-21. Preprints2024, 2024051769. https://doi.org/10.20944/preprints202405.1769.v1
Al Ebrahim, R. N.; Alekseeva, M. G.; Bazhenov, S. V.; Fomin, V. V.; Mavletova, D. A.; Nesterov, A. A.; Poluektova, E. U.; Danilenko, V. N.; Manukhov, I. V. ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus fermentum U-21. Preprints 2024, 2024051769. https://doi.org/10.20944/preprints202405.1769.v1
Al Ebrahim, R. N.; Alekseeva, M. G.; Bazhenov, S. V.; Fomin, V. V.; Mavletova, D. A.; Nesterov, A. A.; Poluektova, E. U.; Danilenko, V. N.; Manukhov, I. V. ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus fermentum U-21. Preprints2024, 2024051769. https://doi.org/10.20944/preprints202405.1769.v1
APA Style
Al Ebrahim, R. N., Alekseeva, M. G., Bazhenov, S. V., Fomin, V. V., Mavletova, D. A., Nesterov, A. A., Poluektova, E. U., Danilenko, V. N., & Manukhov, I. V. (2024). ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus fermentum U-21. Preprints. https://doi.org/10.20944/preprints202405.1769.v1
Chicago/Turabian Style
Al Ebrahim, R. N., Valeriy N. Danilenko and Ilya V. Manukhov. 2024 "ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus fermentum U-21" Preprints. https://doi.org/10.20944/preprints202405.1769.v1
Abstract
Strain L. fermentum U-21 secretes chaperones into the medium and it is considered as the candidate for the development of drugs, so-called disaggregases, for Parkinson’s disease therapy. This study is devoted to characterization of secreted protein encoded by C0965_000195 locus. Analysis of sequence and predicted structure of the protein encoded by C0965_000195 allows us to attribute it to the ClpL, homologs of which are known to be chaperones. The chaperone activity of ClpL L. fermentum U-21 was evaluated in vivo by refolding of differing in thermostability luciferases from Aliivibrio fischeri and Photorhabdus luminescens in Escherichia coli cells. It was observed that clpL from L. fermentum U-21 can compensate for the deficiency in the clpB gene and enhance the ability to refold thermodenatured proteins in clpB- cells. In vitro experiments have demonstrated the ability of a spent culture medium containing proteins secreted by L. fermentum U-21 cells, including ClpL, to prevent thermodenaturation of luciferases partially.We suggest that the ClpL protein from L. fermentum U-21 strain, which exhibits disaggregase properties against aggregating proteins, may be one of the clue components that play a role in the pharmabiotic properties of this strain.
Keywords
ClpL; Chaperon; Luciferases
Subject
Biology and Life Sciences, Biology and Biotechnology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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