Exploring proteins within the coccolith matrix
Abstract Coccolithophores comprise a major component of the oceanic carbon cycle. These unicellular algae produce ornate structures made of calcium carbonate, termed coccoliths, representing ~ 50% of calcite production in the open ocean. The exact molecular mechanisms which direct and control coccol...
Saved in:
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2024-12-01
|
| Series: | Scientific Reports |
| Subjects: | |
| Online Access: | https://doi.org/10.1038/s41598-024-83052-9 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849343312188669952 |
|---|---|
| author | Craig J. Dedman Nishant Chauhan Alba González-Lanchas Chloë Baldreki Adam A. Dowle Tony R. Larson Renee B. Y. Lee Rosalind E. M. Rickaby |
| author_facet | Craig J. Dedman Nishant Chauhan Alba González-Lanchas Chloë Baldreki Adam A. Dowle Tony R. Larson Renee B. Y. Lee Rosalind E. M. Rickaby |
| author_sort | Craig J. Dedman |
| collection | DOAJ |
| description | Abstract Coccolithophores comprise a major component of the oceanic carbon cycle. These unicellular algae produce ornate structures made of calcium carbonate, termed coccoliths, representing ~ 50% of calcite production in the open ocean. The exact molecular mechanisms which direct and control coccolith formation are unknown. In this study, we report on the presence and functional features of proteins within the coccoliths produced by a range of model coccolithophore species including: the globally abundant and well-studied Gephyrocapsa huxleyi (formerly Emiliania huxleyi) and related Gephyrocapsa oceanica, as well as the larger and more heavily calcified Coccolithus braarudii. Protein features were compared between species and against biomineralisation proteins previously identified in other marine calcifying organisms. Notably, several protein features were consistently seen across the examined coccolithophore species, including the cell signalling 14-3-3 domain, chromosome segregation SMC ATPase domain, as well as proteins involved in protein processing and protease inhibition. The copper-binding cupredoxin domain was observed in both Gephyrocapsa species, as well as other marine calcifiers, suggestive of a requirement of Cu in biomineralisation. Building consensus with existing work, we highlight the pentapeptide repeat as a feature which is associated with the coccolith matrix, being identified in all three examined species, and propose that this structural motif may play a role in controlling coccolith growth. This preliminary study provides insight towards the functional diversity of calcification machinery in coccolithophores and presents a number of candidates for future research towards understanding the biochemical controls which direct coccolithogenesis. |
| format | Article |
| id | doaj-art-45f76d40fc554d168fa50e27749348a6 |
| institution | Kabale University |
| issn | 2045-2322 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj-art-45f76d40fc554d168fa50e27749348a62025-08-20T03:43:02ZengNature PortfolioScientific Reports2045-23222024-12-0114111610.1038/s41598-024-83052-9Exploring proteins within the coccolith matrixCraig J. Dedman0Nishant Chauhan1Alba González-Lanchas2Chloë Baldreki3Adam A. Dowle4Tony R. Larson5Renee B. Y. Lee6Rosalind E. M. Rickaby7Department of Earth Sciences, University of OxfordDepartment of Earth Sciences, University of OxfordDepartment of Earth Sciences, University of OxfordDepartment of Biology, Bioscience Technology Facility, University of YorkDepartment of Biology, Bioscience Technology Facility, University of YorkDepartment of Biology, Bioscience Technology Facility, University of YorkSchool of Biological Sciences, University of ReadingDepartment of Earth Sciences, University of OxfordAbstract Coccolithophores comprise a major component of the oceanic carbon cycle. These unicellular algae produce ornate structures made of calcium carbonate, termed coccoliths, representing ~ 50% of calcite production in the open ocean. The exact molecular mechanisms which direct and control coccolith formation are unknown. In this study, we report on the presence and functional features of proteins within the coccoliths produced by a range of model coccolithophore species including: the globally abundant and well-studied Gephyrocapsa huxleyi (formerly Emiliania huxleyi) and related Gephyrocapsa oceanica, as well as the larger and more heavily calcified Coccolithus braarudii. Protein features were compared between species and against biomineralisation proteins previously identified in other marine calcifying organisms. Notably, several protein features were consistently seen across the examined coccolithophore species, including the cell signalling 14-3-3 domain, chromosome segregation SMC ATPase domain, as well as proteins involved in protein processing and protease inhibition. The copper-binding cupredoxin domain was observed in both Gephyrocapsa species, as well as other marine calcifiers, suggestive of a requirement of Cu in biomineralisation. Building consensus with existing work, we highlight the pentapeptide repeat as a feature which is associated with the coccolith matrix, being identified in all three examined species, and propose that this structural motif may play a role in controlling coccolith growth. This preliminary study provides insight towards the functional diversity of calcification machinery in coccolithophores and presents a number of candidates for future research towards understanding the biochemical controls which direct coccolithogenesis.https://doi.org/10.1038/s41598-024-83052-9BiomineralisationPhytoplanktonCalcificationCoccolithophoreCarbon cycle |
| spellingShingle | Craig J. Dedman Nishant Chauhan Alba González-Lanchas Chloë Baldreki Adam A. Dowle Tony R. Larson Renee B. Y. Lee Rosalind E. M. Rickaby Exploring proteins within the coccolith matrix Scientific Reports Biomineralisation Phytoplankton Calcification Coccolithophore Carbon cycle |
| title | Exploring proteins within the coccolith matrix |
| title_full | Exploring proteins within the coccolith matrix |
| title_fullStr | Exploring proteins within the coccolith matrix |
| title_full_unstemmed | Exploring proteins within the coccolith matrix |
| title_short | Exploring proteins within the coccolith matrix |
| title_sort | exploring proteins within the coccolith matrix |
| topic | Biomineralisation Phytoplankton Calcification Coccolithophore Carbon cycle |
| url | https://doi.org/10.1038/s41598-024-83052-9 |
| work_keys_str_mv | AT craigjdedman exploringproteinswithinthecoccolithmatrix AT nishantchauhan exploringproteinswithinthecoccolithmatrix AT albagonzalezlanchas exploringproteinswithinthecoccolithmatrix AT chloebaldreki exploringproteinswithinthecoccolithmatrix AT adamadowle exploringproteinswithinthecoccolithmatrix AT tonyrlarson exploringproteinswithinthecoccolithmatrix AT reneebylee exploringproteinswithinthecoccolithmatrix AT rosalindemrickaby exploringproteinswithinthecoccolithmatrix |