Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications
The catalytic performance of the major CO 2 -assimilating enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), restricts photosynthetic productivity. Natural diversity in the catalytic properties of Rubisco indicates possibilities for improvement. Oceanic phytoplankton contain some of...
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Online Access: | https://hdl.handle.net/10037/24717 https://doi.org/10.1074/jbc.RA118.003518 |
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ftunivtroemsoe:oai:munin.uit.no:10037/24717 2023-05-15T14:26:19+02:00 Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications Valegård, Karin Andralojc, P. John Haslam, Richard P. Pearce, F. Grant Eriksen, Gunilla Kristina Madgwick, Pippa J. Kristoffersen, Anne Karin van Lun, Michiel Klein, Uwe Eilertsen, Hans Christian Parry, Martin A.J. Andersson, Inger 2018-06-20 https://hdl.handle.net/10037/24717 https://doi.org/10.1074/jbc.RA118.003518 eng eng Elsevier Journal of Biological Chemistry Valegård, Andralojc PJ, Haslam, Pearce, Eriksen GKE, Madgwick PJ, Kristoffersen AK, van Lun, Klein U, Eilertsen HC, Parry, Andersson I. Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications. Journal of Biological Chemistry. 2018;293(34):13033-13043 FRIDAID 1607629 doi:10.1074/jbc.RA118.003518 0021-9258 1083-351X https://hdl.handle.net/10037/24717 openAccess Copyright 2018 The Author(s) Journal article Tidsskriftartikkel Peer reviewed publishedVersion 2018 ftunivtroemsoe https://doi.org/10.1074/jbc.RA118.003518 2022-04-06T22:58:30Z The catalytic performance of the major CO 2 -assimilating enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), restricts photosynthetic productivity. Natural diversity in the catalytic properties of Rubisco indicates possibilities for improvement. Oceanic phytoplankton contain some of the most efficient Rubisco enzymes, and diatoms in particular are responsible for a significant proportion of total marine primary production as well as being a major source of CO 2 sequestration in polar cold waters. Until now, the biochemical properties and three-dimensional structures of Rubisco from diatoms were unknown. Here, diatoms from arctic waters were collected, cultivated, and analyzed for their CO 2 -fixing capability. We characterized the kinetic properties of five and determined the crystal structures of four Rubiscos selected for their high CO 2 -fixing efficiency. The DNA sequences of the rbcL and rbcS genes of the selected diatoms were similar, reflecting their close phylogenetic relationship. The Vmax and Km for the oxygenase and carboxylase activities at 25 °C and the specificity factors (Sc/o) at 15, 25, and 35 °C were determined. The Sc/o values were high, approaching those of mono- and dicot plants, thus exhibiting good selectivity for CO 2 relative to O 2 . Structurally, diatom Rubiscos belong to form I C/D, containing small subunits characterized by a short βA–βB loop and a C-terminal extension that forms a β-hairpin structure (βE–βF loop). Of note, the diatom Rubiscos featured a number of posttranslational modifications of the large subunit, including 4-hydroxyproline, β-hydroxyleucine, hydroxylated and nitrosylated cysteine, mono- and dihydroxylated lysine, and trimethylated lysine. Our studies suggest adaptation toward achieving efficient CO 2 fixation in arctic diatom Rubiscos. Article in Journal/Newspaper Arctic Arctic Phytoplankton University of Tromsø: Munin Open Research Archive Arctic Journal of Biological Chemistry 293 34 13033 13043 |
institution |
Open Polar |
collection |
University of Tromsø: Munin Open Research Archive |
op_collection_id |
ftunivtroemsoe |
language |
English |
description |
The catalytic performance of the major CO 2 -assimilating enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), restricts photosynthetic productivity. Natural diversity in the catalytic properties of Rubisco indicates possibilities for improvement. Oceanic phytoplankton contain some of the most efficient Rubisco enzymes, and diatoms in particular are responsible for a significant proportion of total marine primary production as well as being a major source of CO 2 sequestration in polar cold waters. Until now, the biochemical properties and three-dimensional structures of Rubisco from diatoms were unknown. Here, diatoms from arctic waters were collected, cultivated, and analyzed for their CO 2 -fixing capability. We characterized the kinetic properties of five and determined the crystal structures of four Rubiscos selected for their high CO 2 -fixing efficiency. The DNA sequences of the rbcL and rbcS genes of the selected diatoms were similar, reflecting their close phylogenetic relationship. The Vmax and Km for the oxygenase and carboxylase activities at 25 °C and the specificity factors (Sc/o) at 15, 25, and 35 °C were determined. The Sc/o values were high, approaching those of mono- and dicot plants, thus exhibiting good selectivity for CO 2 relative to O 2 . Structurally, diatom Rubiscos belong to form I C/D, containing small subunits characterized by a short βA–βB loop and a C-terminal extension that forms a β-hairpin structure (βE–βF loop). Of note, the diatom Rubiscos featured a number of posttranslational modifications of the large subunit, including 4-hydroxyproline, β-hydroxyleucine, hydroxylated and nitrosylated cysteine, mono- and dihydroxylated lysine, and trimethylated lysine. Our studies suggest adaptation toward achieving efficient CO 2 fixation in arctic diatom Rubiscos. |
format |
Article in Journal/Newspaper |
author |
Valegård, Karin Andralojc, P. John Haslam, Richard P. Pearce, F. Grant Eriksen, Gunilla Kristina Madgwick, Pippa J. Kristoffersen, Anne Karin van Lun, Michiel Klein, Uwe Eilertsen, Hans Christian Parry, Martin A.J. Andersson, Inger |
spellingShingle |
Valegård, Karin Andralojc, P. John Haslam, Richard P. Pearce, F. Grant Eriksen, Gunilla Kristina Madgwick, Pippa J. Kristoffersen, Anne Karin van Lun, Michiel Klein, Uwe Eilertsen, Hans Christian Parry, Martin A.J. Andersson, Inger Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications |
author_facet |
Valegård, Karin Andralojc, P. John Haslam, Richard P. Pearce, F. Grant Eriksen, Gunilla Kristina Madgwick, Pippa J. Kristoffersen, Anne Karin van Lun, Michiel Klein, Uwe Eilertsen, Hans Christian Parry, Martin A.J. Andersson, Inger |
author_sort |
Valegård, Karin |
title |
Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications |
title_short |
Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications |
title_full |
Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications |
title_fullStr |
Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications |
title_full_unstemmed |
Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications |
title_sort |
structural and functional analyses of rubisco from arctic diatom species reveal unusual posttranslational modifications |
publisher |
Elsevier |
publishDate |
2018 |
url |
https://hdl.handle.net/10037/24717 https://doi.org/10.1074/jbc.RA118.003518 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic Arctic Phytoplankton |
genre_facet |
Arctic Arctic Phytoplankton |
op_relation |
Journal of Biological Chemistry Valegård, Andralojc PJ, Haslam, Pearce, Eriksen GKE, Madgwick PJ, Kristoffersen AK, van Lun, Klein U, Eilertsen HC, Parry, Andersson I. Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications. Journal of Biological Chemistry. 2018;293(34):13033-13043 FRIDAID 1607629 doi:10.1074/jbc.RA118.003518 0021-9258 1083-351X https://hdl.handle.net/10037/24717 |
op_rights |
openAccess Copyright 2018 The Author(s) |
op_doi |
https://doi.org/10.1074/jbc.RA118.003518 |
container_title |
Journal of Biological Chemistry |
container_volume |
293 |
container_issue |
34 |
container_start_page |
13033 |
op_container_end_page |
13043 |
_version_ |
1766298821607817216 |