CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus
International audience CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence CC A at tRNA 3'-ends. Recently, we could reveal that cold adaptation of such a polymerase is not only achieved at the expense of enzyme stability, but also at the cost of polymerizat...
Published in: | Computational and Structural Biotechnology Journal |
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Format: | Article in Journal/Newspaper |
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Online Access: | https://hal.science/hal-03419675 https://hal.science/hal-03419675/document https://hal.science/hal-03419675/file/Sauter%20C%20-CCA-addition%20in%20the%20cold-%20Structural%20characterization%20of%20the%20psychrophilic%20CCA-adding%20enzyme%20from%20the%20permafrost%20bacterium%20Planococcus%20halocryophilus.pdf https://doi.org/10.1016/j.csbj.2021.10.018 |
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ftanrparis:oai:HAL:hal-03419675v1 2024-09-15T18:29:57+00:00 CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus de Wijn, Raphaël Rollet, Kévin Ernst, Felix G.M. Wellner, Karolin Betat, Heike Mörl, Mario Sauter, Claude Architecture et Réactivité de l'ARN (ARN) Institut de biologie moléculaire et cellulaire (IBMC) Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS) ANR-10-LABX-0036,NetRNA,Network of regulatory RNAs across kingdoms and dynamical responses to biotic and abiotic stresses.(2010) 2021-10-21 https://hal.science/hal-03419675 https://hal.science/hal-03419675/document https://hal.science/hal-03419675/file/Sauter%20C%20-CCA-addition%20in%20the%20cold-%20Structural%20characterization%20of%20the%20psychrophilic%20CCA-adding%20enzyme%20from%20the%20permafrost%20bacterium%20Planococcus%20halocryophilus.pdf https://doi.org/10.1016/j.csbj.2021.10.018 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.csbj.2021.10.018 hal-03419675 https://hal.science/hal-03419675 https://hal.science/hal-03419675/document https://hal.science/hal-03419675/file/Sauter%20C%20-CCA-addition%20in%20the%20cold-%20Structural%20characterization%20of%20the%20psychrophilic%20CCA-adding%20enzyme%20from%20the%20permafrost%20bacterium%20Planococcus%20halocryophilus.pdf doi:10.1016/j.csbj.2021.10.018 info:eu-repo/semantics/OpenAccess ISSN: 2001-0370 Computational and Structural Biotechnology Journal https://hal.science/hal-03419675 Computational and Structural Biotechnology Journal, 2021, 19, pp.5845 - 5855. ⟨10.1016/j.csbj.2021.10.018⟩ [SDV]Life Sciences [q-bio] [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology info:eu-repo/semantics/article Journal articles 2021 ftanrparis https://doi.org/10.1016/j.csbj.2021.10.018 2024-07-12T11:04:36Z International audience CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence CC A at tRNA 3'-ends. Recently, we could reveal that cold adaptation of such a polymerase is not only achieved at the expense of enzyme stability, but also at the cost of polymerization fidelity. Enzymes from psychrophilic organisms usually show an increased structural flexibility to enable catalysis at low temperatures. Here, polymerases face a dilemma, as there is a discrepancy between the need for a tightly controlled flexibility during polymerization and an increased flexibility as strategy for cold adaptation. Based on structural and biochemical analyses, we contribute to clarify the cold adaptation strategy of the psychrophilic CCA-adding enzyme from Planococcus halocryophilus, a gram-positive bacterium thriving in the arctic permafrost at low temperatures down to À15°C. A comparison with the closely related enzyme from the thermophilic bacterium Geobacillus stearothermophilus reveals several features of cold adaptation-a significantly reduced amount of alpha-helical elements in the C-terminal tRNA-binding region and a structural adaptation in one of the highly conserved catalytic core motifs located in the N-terminal catalytic core of the enzyme. Article in Journal/Newspaper permafrost Portail HAL-ANR (Agence Nationale de la Recherche) Computational and Structural Biotechnology Journal 19 5845 5855 |
institution |
Open Polar |
collection |
Portail HAL-ANR (Agence Nationale de la Recherche) |
op_collection_id |
ftanrparis |
language |
English |
topic |
[SDV]Life Sciences [q-bio] [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
spellingShingle |
[SDV]Life Sciences [q-bio] [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology de Wijn, Raphaël Rollet, Kévin Ernst, Felix G.M. Wellner, Karolin Betat, Heike Mörl, Mario Sauter, Claude CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus |
topic_facet |
[SDV]Life Sciences [q-bio] [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
description |
International audience CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence CC A at tRNA 3'-ends. Recently, we could reveal that cold adaptation of such a polymerase is not only achieved at the expense of enzyme stability, but also at the cost of polymerization fidelity. Enzymes from psychrophilic organisms usually show an increased structural flexibility to enable catalysis at low temperatures. Here, polymerases face a dilemma, as there is a discrepancy between the need for a tightly controlled flexibility during polymerization and an increased flexibility as strategy for cold adaptation. Based on structural and biochemical analyses, we contribute to clarify the cold adaptation strategy of the psychrophilic CCA-adding enzyme from Planococcus halocryophilus, a gram-positive bacterium thriving in the arctic permafrost at low temperatures down to À15°C. A comparison with the closely related enzyme from the thermophilic bacterium Geobacillus stearothermophilus reveals several features of cold adaptation-a significantly reduced amount of alpha-helical elements in the C-terminal tRNA-binding region and a structural adaptation in one of the highly conserved catalytic core motifs located in the N-terminal catalytic core of the enzyme. |
author2 |
Architecture et Réactivité de l'ARN (ARN) Institut de biologie moléculaire et cellulaire (IBMC) Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS) ANR-10-LABX-0036,NetRNA,Network of regulatory RNAs across kingdoms and dynamical responses to biotic and abiotic stresses.(2010) |
format |
Article in Journal/Newspaper |
author |
de Wijn, Raphaël Rollet, Kévin Ernst, Felix G.M. Wellner, Karolin Betat, Heike Mörl, Mario Sauter, Claude |
author_facet |
de Wijn, Raphaël Rollet, Kévin Ernst, Felix G.M. Wellner, Karolin Betat, Heike Mörl, Mario Sauter, Claude |
author_sort |
de Wijn, Raphaël |
title |
CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus |
title_short |
CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus |
title_full |
CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus |
title_fullStr |
CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus |
title_full_unstemmed |
CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus |
title_sort |
cca-addition in the cold: structural characterization of the psychrophilic cca-adding enzyme from the permafrost bacterium planococcus halocryophilus |
publisher |
HAL CCSD |
publishDate |
2021 |
url |
https://hal.science/hal-03419675 https://hal.science/hal-03419675/document https://hal.science/hal-03419675/file/Sauter%20C%20-CCA-addition%20in%20the%20cold-%20Structural%20characterization%20of%20the%20psychrophilic%20CCA-adding%20enzyme%20from%20the%20permafrost%20bacterium%20Planococcus%20halocryophilus.pdf https://doi.org/10.1016/j.csbj.2021.10.018 |
genre |
permafrost |
genre_facet |
permafrost |
op_source |
ISSN: 2001-0370 Computational and Structural Biotechnology Journal https://hal.science/hal-03419675 Computational and Structural Biotechnology Journal, 2021, 19, pp.5845 - 5855. ⟨10.1016/j.csbj.2021.10.018⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.csbj.2021.10.018 hal-03419675 https://hal.science/hal-03419675 https://hal.science/hal-03419675/document https://hal.science/hal-03419675/file/Sauter%20C%20-CCA-addition%20in%20the%20cold-%20Structural%20characterization%20of%20the%20psychrophilic%20CCA-adding%20enzyme%20from%20the%20permafrost%20bacterium%20Planococcus%20halocryophilus.pdf doi:10.1016/j.csbj.2021.10.018 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.csbj.2021.10.018 |
container_title |
Computational and Structural Biotechnology Journal |
container_volume |
19 |
container_start_page |
5845 |
op_container_end_page |
5855 |
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1810471435847598080 |