Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications
The catalytic performance of the major CO2-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 th...
Published in: | Journal of Biological Chemistry |
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2018
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Online Access: | https://eprints.lancs.ac.uk/id/eprint/126079/ https://eprints.lancs.ac.uk/id/eprint/126079/1/003518R1_Merged_PDF.pdf https://doi.org/10.1074/jbc.RA118.003518 |
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ftulancaster:oai:eprints.lancs.ac.uk:126079 2023-12-17T10:23:27+01:00 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 K Madgwick, Pippa J Kristoffersen, Anne K van Lun, Michiel Klein, Uwe Eilertsen, Hans C Andersson, Inger Parry, Martin A J 2018-08-24 application/pdf https://eprints.lancs.ac.uk/id/eprint/126079/ https://eprints.lancs.ac.uk/id/eprint/126079/1/003518R1_Merged_PDF.pdf https://doi.org/10.1074/jbc.RA118.003518 en eng https://eprints.lancs.ac.uk/id/eprint/126079/1/003518R1_Merged_PDF.pdf Valegård, Karin and Andralojc, P John and Haslam, Richard P and Pearce, F Grant and Eriksen, Gunilla K and Madgwick, Pippa J and Kristoffersen, Anne K and van Lun, Michiel and Klein, Uwe and Eilertsen, Hans C and Andersson, Inger and Parry, Martin A J (2018) Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications. Journal of Biological Chemistry, 293. pp. 13033-13043. ISSN 0021-9258 creative_commons_attribution_noncommercial_4_0_international_license Journal Article PeerReviewed 2018 ftulancaster https://doi.org/10.1074/jbc.RA118.003518 2023-11-23T23:18:15Z The catalytic performance of the major CO2-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 CO2 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 CO2 fixing capability. We characterized the kinetic properties of five, and determined the crystal structures of four Rubiscos selected for their high CO2-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 CO2 relative to O2 Structurally, diatom Rubiscos belong to Form I C/D, containing small subunits characterised by a short βA-βB loop and a carboxy-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-hydroxy-proline, betahydroxyleucine, hydroxylated, and nitrosylated cysteine, mono-, and di-hydroxylated lysine, and tri-methylated lysine. Our studies suggest adaptation toward achieving efficient CO2-fixation in Arctic diatom Rubiscos. Article in Journal/Newspaper Arctic Arctic Phytoplankton Lancaster University: Lancaster Eprints Arctic Journal of Biological Chemistry 293 34 13033 13043 |
institution |
Open Polar |
collection |
Lancaster University: Lancaster Eprints |
op_collection_id |
ftulancaster |
language |
English |
description |
The catalytic performance of the major CO2-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 CO2 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 CO2 fixing capability. We characterized the kinetic properties of five, and determined the crystal structures of four Rubiscos selected for their high CO2-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 CO2 relative to O2 Structurally, diatom Rubiscos belong to Form I C/D, containing small subunits characterised by a short βA-βB loop and a carboxy-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-hydroxy-proline, betahydroxyleucine, hydroxylated, and nitrosylated cysteine, mono-, and di-hydroxylated lysine, and tri-methylated lysine. Our studies suggest adaptation toward achieving efficient CO2-fixation in Arctic diatom Rubiscos. |
format |
Article in Journal/Newspaper |
author |
Valegård, Karin Andralojc, P John Haslam, Richard P Pearce, F Grant Eriksen, Gunilla K Madgwick, Pippa J Kristoffersen, Anne K van Lun, Michiel Klein, Uwe Eilertsen, Hans C Andersson, Inger Parry, Martin A J |
spellingShingle |
Valegård, Karin Andralojc, P John Haslam, Richard P Pearce, F Grant Eriksen, Gunilla K Madgwick, Pippa J Kristoffersen, Anne K van Lun, Michiel Klein, Uwe Eilertsen, Hans C Andersson, Inger Parry, Martin A J 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 K Madgwick, Pippa J Kristoffersen, Anne K van Lun, Michiel Klein, Uwe Eilertsen, Hans C Andersson, Inger Parry, Martin A J |
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 |
publishDate |
2018 |
url |
https://eprints.lancs.ac.uk/id/eprint/126079/ https://eprints.lancs.ac.uk/id/eprint/126079/1/003518R1_Merged_PDF.pdf https://doi.org/10.1074/jbc.RA118.003518 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic Arctic Phytoplankton |
genre_facet |
Arctic Arctic Phytoplankton |
op_relation |
https://eprints.lancs.ac.uk/id/eprint/126079/1/003518R1_Merged_PDF.pdf Valegård, Karin and Andralojc, P John and Haslam, Richard P and Pearce, F Grant and Eriksen, Gunilla K and Madgwick, Pippa J and Kristoffersen, Anne K and van Lun, Michiel and Klein, Uwe and Eilertsen, Hans C and Andersson, Inger and Parry, Martin A J (2018) Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications. Journal of Biological Chemistry, 293. pp. 13033-13043. ISSN 0021-9258 |
op_rights |
creative_commons_attribution_noncommercial_4_0_international_license |
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_ |
1785557988978720768 |