Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system

The Hsp100 family member ClpB is a protein disaggregase which solubilizes and reactivates stress-induced protein aggregates in cooperation with the DnaK/Hsp70 chaperone system. In the pathogenic bacterium Francisella tularensis, ClpB is involved in type VI secretion system (T6SS) disassembly through...

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Autores principales: Mushtaq, Ameeq Ul, Ådén, Jörgen, Alam, Athar, Sjöstedt, Anders, Gröbner, Gerhard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068650/
https://www.ncbi.nlm.nih.gov/pubmed/34985724
http://dx.doi.org/10.1007/s12104-021-10062-3
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author Mushtaq, Ameeq Ul
Ådén, Jörgen
Alam, Athar
Sjöstedt, Anders
Gröbner, Gerhard
author_facet Mushtaq, Ameeq Ul
Ådén, Jörgen
Alam, Athar
Sjöstedt, Anders
Gröbner, Gerhard
author_sort Mushtaq, Ameeq Ul
collection PubMed
description The Hsp100 family member ClpB is a protein disaggregase which solubilizes and reactivates stress-induced protein aggregates in cooperation with the DnaK/Hsp70 chaperone system. In the pathogenic bacterium Francisella tularensis, ClpB is involved in type VI secretion system (T6SS) disassembly through depolymerization of the IglA-IglB sheath. This leads to recycling and reassembly of T6SS components and this process is essential for the virulence of the bacterium. Here we report the backbone chemical shift assignments and (15)N relaxation-based backbone dynamics of the N-terminal substrate-binding domain of ClpB (1-156). SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s12104-021-10062-3.
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spelling pubmed-90686502022-05-07 Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system Mushtaq, Ameeq Ul Ådén, Jörgen Alam, Athar Sjöstedt, Anders Gröbner, Gerhard Biomol NMR Assign Article The Hsp100 family member ClpB is a protein disaggregase which solubilizes and reactivates stress-induced protein aggregates in cooperation with the DnaK/Hsp70 chaperone system. In the pathogenic bacterium Francisella tularensis, ClpB is involved in type VI secretion system (T6SS) disassembly through depolymerization of the IglA-IglB sheath. This leads to recycling and reassembly of T6SS components and this process is essential for the virulence of the bacterium. Here we report the backbone chemical shift assignments and (15)N relaxation-based backbone dynamics of the N-terminal substrate-binding domain of ClpB (1-156). SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s12104-021-10062-3. Springer Netherlands 2022-01-05 2022 /pmc/articles/PMC9068650/ /pubmed/34985724 http://dx.doi.org/10.1007/s12104-021-10062-3 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Mushtaq, Ameeq Ul
Ådén, Jörgen
Alam, Athar
Sjöstedt, Anders
Gröbner, Gerhard
Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system
title Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system
title_full Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system
title_fullStr Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system
title_full_unstemmed Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system
title_short Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system
title_sort backbone chemical shift assignment and dynamics of the n-terminal domain of clpb from francisella tularensis type vi secretion system
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9068650/
https://www.ncbi.nlm.nih.gov/pubmed/34985724
http://dx.doi.org/10.1007/s12104-021-10062-3
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