Novel protein CcmS is required for stabilization of the assembly of β-carboxysome in Synechocystis sp. strain PCC 6803
© 2023 The Authors. New Phytologist © 2023 New Phytologist Foundation.
| Veröffentlicht in: | The New phytologist. - 1979. - 239(2023), 4 vom: 05. Aug., Seite 1266-1280 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2023
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| Zugriff auf das übergeordnete Werk: | The New phytologist |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't CcmK1 CcmM CcmS carbon concentration mechanism carboxysome Carbon Dioxide 142M471B3J Bacterial Proteins mehr... |
| Zusammenfassung: | © 2023 The Authors. New Phytologist © 2023 New Phytologist Foundation. The carboxysome plays an essential role in the carbon concentration mechanism in cyanobacteria. Although significant progress has been made in the structural analysis of the carboxysome, little is still known about its biosynthesis. We identified slr1911, a gene encoding a protein of unknown function in cyanobacterium Synechocystis sp. Strain PCC 6803 (Syn6803), which we termed ccmS by screening a low CO2 -sensitive mutant. CcmS interacts with CcmK1 and CcmM. The former is a shell protein of the β-carboxysome and the latter is a crucial component of the β-carboxysome, which is responsible for aggregating RuBisCO and recruiting shell proteins. The deletion of ccmS lowers the accumulation and assembly of CcmK1, resulting in aberrant carboxysomes, suppressed photosynthetic capacities, and leads to a slow growth phenotype, especially under CO2 -limited conditions. These observations suggest that CcmS stabilizes the assembly of the β-carboxysome shell and likely connects the carboxysome core with the shell. Our results provide a molecular view of the role played by CcmS in the formation of the β-carboxysome and its function in Syn6803 |
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| Beschreibung: | Date Completed 14.07.2023 Date Revised 18.07.2023 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1469-8137 |
| DOI: | 10.1111/nph.19016 |