Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
The proteomes expressed at 4°C and 18°C by the psychrophilic Antarctic bacterium Pseudoalteromonas haloplanktis have been compared using two-dimensional differential in-gel electrophoresis, showing that translation, protein folding, membrane integrity and anti-oxidant activities are upregulated at 4...
Published in: | Molecular Microbiology |
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2010
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ftvliz:oai:oma.vliz.be:280771 2023-05-15T13:54:11+02:00 Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 Piette, F. D'Amico, S. Struvay, C. Mazzucchelli, G. Renaut, J. Tutino, M.L. Danchin, A. Leprince, P. Feller, G. 2010 application/pdf https://www.vliz.be/imisdocs/publications/296041.pdf en eng info:eu-repo/semantics/altIdentifier/wos/000276036000009 info:eu-repo/semantics/altIdentifier/doi/doi.org/10.1111/j.1365-2958.2010.07084.x https://www.vliz.be/imisdocs/publications/296041.pdf info:eu-repo/semantics/openAccess %3Ci%3EMol.+Microbiol.+76%281%29%3C%2Fi%3E%3A+120-132.+%3Ca+href%3D%22https%3A%2F%2Fdx.doi.org%2F10.1111%2Fj.1365-2958.2010.07084.x%22+target%3D%22_blank%22%3Ehttps%3A%2F%2Fdx.doi.org%2F10.1111%2Fj.1365-2958.2010.07084.x%3C%2Fa%3E info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 2010 ftvliz https://doi.org/10.1111/j.1365-2958.2010.07084.x 2022-05-01T10:44:45Z The proteomes expressed at 4°C and 18°C by the psychrophilic Antarctic bacterium Pseudoalteromonas haloplanktis have been compared using two-dimensional differential in-gel electrophoresis, showing that translation, protein folding, membrane integrity and anti-oxidant activities are upregulated at 4°C. This proteomic analysis revealed that the trigger factor is the main upregulated protein at low temperature. The trigger factor is the first molecular chaperone interacting with virtually all newly synthesized polypeptides on the ribosome and also possesses a peptidyl-prolyl cis-trans isomerase activity. This suggests that protein folding at low temperatures is a rate-limiting step for bacterial growth in cold environments. It is proposed that the psychrophilic trigger factor rescues the chaperone function as both DnaK and GroEL (the major bacterial chaperones but also heat-shock proteins) are downregulated at 4°C. The recombinant psychrophilic trigger factor is a monomer that displays unusually low conformational stability with a Tm value of 33°C, suggesting that the essential chaperone function requires considerable flexibility and dynamics to compensate for the reduction of molecular motions at freezing temperatures. Its chaperone activity is strongly temperature-dependent and requires near-zero temperature to stably bind a model-unfolded polypeptide. Article in Journal/Newspaper Antarc* Antarctic Flanders Marine Institute (VLIZ): Open Marine Archive (OMA) Antarctic The Antarctic Molecular Microbiology 76 1 120 132 |
institution |
Open Polar |
collection |
Flanders Marine Institute (VLIZ): Open Marine Archive (OMA) |
op_collection_id |
ftvliz |
language |
English |
description |
The proteomes expressed at 4°C and 18°C by the psychrophilic Antarctic bacterium Pseudoalteromonas haloplanktis have been compared using two-dimensional differential in-gel electrophoresis, showing that translation, protein folding, membrane integrity and anti-oxidant activities are upregulated at 4°C. This proteomic analysis revealed that the trigger factor is the main upregulated protein at low temperature. The trigger factor is the first molecular chaperone interacting with virtually all newly synthesized polypeptides on the ribosome and also possesses a peptidyl-prolyl cis-trans isomerase activity. This suggests that protein folding at low temperatures is a rate-limiting step for bacterial growth in cold environments. It is proposed that the psychrophilic trigger factor rescues the chaperone function as both DnaK and GroEL (the major bacterial chaperones but also heat-shock proteins) are downregulated at 4°C. The recombinant psychrophilic trigger factor is a monomer that displays unusually low conformational stability with a Tm value of 33°C, suggesting that the essential chaperone function requires considerable flexibility and dynamics to compensate for the reduction of molecular motions at freezing temperatures. Its chaperone activity is strongly temperature-dependent and requires near-zero temperature to stably bind a model-unfolded polypeptide. |
format |
Article in Journal/Newspaper |
author |
Piette, F. D'Amico, S. Struvay, C. Mazzucchelli, G. Renaut, J. Tutino, M.L. Danchin, A. Leprince, P. Feller, G. |
spellingShingle |
Piette, F. D'Amico, S. Struvay, C. Mazzucchelli, G. Renaut, J. Tutino, M.L. Danchin, A. Leprince, P. Feller, G. Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 |
author_facet |
Piette, F. D'Amico, S. Struvay, C. Mazzucchelli, G. Renaut, J. Tutino, M.L. Danchin, A. Leprince, P. Feller, G. |
author_sort |
Piette, F. |
title |
Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 |
title_short |
Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 |
title_full |
Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 |
title_fullStr |
Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 |
title_full_unstemmed |
Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 |
title_sort |
proteomics of life at low temperatures: trigger factor is the primary chaperone in the antarctic bacterium pseudoalteromonas haloplanktis tac125 |
publishDate |
2010 |
url |
https://www.vliz.be/imisdocs/publications/296041.pdf |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
%3Ci%3EMol.+Microbiol.+76%281%29%3C%2Fi%3E%3A+120-132.+%3Ca+href%3D%22https%3A%2F%2Fdx.doi.org%2F10.1111%2Fj.1365-2958.2010.07084.x%22+target%3D%22_blank%22%3Ehttps%3A%2F%2Fdx.doi.org%2F10.1111%2Fj.1365-2958.2010.07084.x%3C%2Fa%3E |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/000276036000009 info:eu-repo/semantics/altIdentifier/doi/doi.org/10.1111/j.1365-2958.2010.07084.x https://www.vliz.be/imisdocs/publications/296041.pdf |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1111/j.1365-2958.2010.07084.x |
container_title |
Molecular Microbiology |
container_volume |
76 |
container_issue |
1 |
container_start_page |
120 |
op_container_end_page |
132 |
_version_ |
1766259846713180160 |