The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance

Hsp70 proteins and their Hsp40 co‐chaperones are essential components of cellular chaperone networks in both prokaryotes and eukaryotes. Here, we performed a genetic analysis to define the protein domains required for the key functions of the major Hsp40/DnaJ protein Sll0897 of the cyanobacterium Sy...

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Autores principales: Düppre, Eva, Schneider, Dirk
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7609799/
https://www.ncbi.nlm.nih.gov/pubmed/32965069
http://dx.doi.org/10.1002/2211-5463.12980
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author Düppre, Eva
Schneider, Dirk
author_facet Düppre, Eva
Schneider, Dirk
author_sort Düppre, Eva
collection PubMed
description Hsp70 proteins and their Hsp40 co‐chaperones are essential components of cellular chaperone networks in both prokaryotes and eukaryotes. Here, we performed a genetic analysis to define the protein domains required for the key functions of the major Hsp40/DnaJ protein Sll0897 of the cyanobacterium Synechocystis sp. PCC6803. The expression of the N‐terminally located J‐ and G/F‐domains is essential and sufficient for the proteins’ fundamental in vivo functions, whereas the presence of the full‐length protein, containing the C‐terminal substrate‐binding domains, is crucial under stress conditions.
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spelling pubmed-76097992020-11-06 The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance Düppre, Eva Schneider, Dirk FEBS Open Bio Research Articles Hsp70 proteins and their Hsp40 co‐chaperones are essential components of cellular chaperone networks in both prokaryotes and eukaryotes. Here, we performed a genetic analysis to define the protein domains required for the key functions of the major Hsp40/DnaJ protein Sll0897 of the cyanobacterium Synechocystis sp. PCC6803. The expression of the N‐terminally located J‐ and G/F‐domains is essential and sufficient for the proteins’ fundamental in vivo functions, whereas the presence of the full‐length protein, containing the C‐terminal substrate‐binding domains, is crucial under stress conditions. John Wiley and Sons Inc. 2020-09-27 /pmc/articles/PMC7609799/ /pubmed/32965069 http://dx.doi.org/10.1002/2211-5463.12980 Text en © 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Düppre, Eva
Schneider, Dirk
The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance
title The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance
title_full The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance
title_fullStr The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance
title_full_unstemmed The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance
title_short The J‐ and G/F‐domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance
title_sort j‐ and g/f‐domains of the major synechocystis dnaj protein sll0897 are sufficient for cell viability but not for heat resistance
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7609799/
https://www.ncbi.nlm.nih.gov/pubmed/32965069
http://dx.doi.org/10.1002/2211-5463.12980
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