CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus
CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence C-C-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...
Published in: | Computational and Structural Biotechnology Journal |
---|---|
Main Authors: | , , , , , , |
Format: | Text |
Language: | English |
Published: |
Research Network of Computational and Structural Biotechnology
2021
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8563995/ https://doi.org/10.1016/j.csbj.2021.10.018 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:8563995 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:8563995 2023-05-15T15:06:07+02:00 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 2021-10-21 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8563995/ https://doi.org/10.1016/j.csbj.2021.10.018 en eng Research Network of Computational and Structural Biotechnology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8563995/ http://dx.doi.org/10.1016/j.csbj.2021.10.018 © 2021 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). CC-BY Comput Struct Biotechnol J Research Article Text 2021 ftpubmed https://doi.org/10.1016/j.csbj.2021.10.018 2021-11-14T01:34:21Z CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence C-C-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 −15 °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. Text Arctic permafrost PubMed Central (PMC) Arctic Computational and Structural Biotechnology Journal 19 5845 5855 |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Research Article |
spellingShingle |
Research Article 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 |
Research Article |
description |
CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence C-C-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 −15 °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. |
format |
Text |
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 |
Research Network of Computational and Structural Biotechnology |
publishDate |
2021 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8563995/ https://doi.org/10.1016/j.csbj.2021.10.018 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic permafrost |
genre_facet |
Arctic permafrost |
op_source |
Comput Struct Biotechnol J |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8563995/ http://dx.doi.org/10.1016/j.csbj.2021.10.018 |
op_rights |
© 2021 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
op_rightsnorm |
CC-BY |
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 |
_version_ |
1766337779033178112 |