A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12
The chloroplast protein CP12, which is widespread in photosynthetic organisms, belongs to the intrinsically disordered proteins family. This small protein (80 amino acid residues long) presents a bias in its composition; it is enriched in charged amino acids, has a small number of hydrophobic residu...
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MDPI AG
2022-07-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/12/8/1047 |
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| author | Cassy Gérard Frédéric Carrière Véronique Receveur-Bréchot Hélène Launay Brigitte Gontero |
| author_facet | Cassy Gérard Frédéric Carrière Véronique Receveur-Bréchot Hélène Launay Brigitte Gontero |
| author_sort | Cassy Gérard |
| collection | DOAJ |
| description | The chloroplast protein CP12, which is widespread in photosynthetic organisms, belongs to the intrinsically disordered proteins family. This small protein (80 amino acid residues long) presents a bias in its composition; it is enriched in charged amino acids, has a small number of hydrophobic residues, and has a high proportion of disorder-promoting residues. More precisely, CP12 is a conditionally disordered proteins (CDP) dependent upon the redox state of its four cysteine residues. During the day, reducing conditions prevail in the chloroplast, and CP12 is fully disordered. Under oxidizing conditions (night), its cysteine residues form two disulfide bridges that confer some stability to some structural elements. Like many CDPs, CP12 plays key roles, and its redox-dependent conditional disorder is important for the main function of CP12: the dark/light regulation of the Calvin-Benson-Bassham (CBB) cycle responsible for CO<sub>2</sub> assimilation. Oxidized CP12 binds to glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase and thereby inhibits their activity. However, recent studies reveal that CP12 may have other functions beyond the CBB cycle regulation. In this review, we report the discovery of this protein, its features as a disordered protein, and the many functions this small protein can have. |
| first_indexed | 2024-03-09T10:00:51Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-09T10:00:51Z |
| publishDate | 2022-07-01 |
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| series | Biomolecules |
| spelling | doaj.art-db1dccd1a1bd4cd6977f23d8c5e9dc5a2023-12-01T23:28:49ZengMDPI AGBiomolecules2218-273X2022-07-01128104710.3390/biom12081047A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12Cassy Gérard0Frédéric Carrière1Véronique Receveur-Bréchot2Hélène Launay3Brigitte Gontero4Aix Marseille Univ, CNRS, BIP, UMR 7281, IMM, FR3479, 31 Chemin J. Aiguier, CEDEX 9, 13 402 Marseille, FranceAix Marseille Univ, CNRS, BIP, UMR 7281, IMM, FR3479, 31 Chemin J. Aiguier, CEDEX 9, 13 402 Marseille, FranceAix Marseille Univ, CNRS, BIP, UMR 7281, IMM, FR3479, 31 Chemin J. Aiguier, CEDEX 9, 13 402 Marseille, FranceAix Marseille Univ, CNRS, BIP, UMR 7281, IMM, FR3479, 31 Chemin J. Aiguier, CEDEX 9, 13 402 Marseille, FranceAix Marseille Univ, CNRS, BIP, UMR 7281, IMM, FR3479, 31 Chemin J. Aiguier, CEDEX 9, 13 402 Marseille, FranceThe chloroplast protein CP12, which is widespread in photosynthetic organisms, belongs to the intrinsically disordered proteins family. This small protein (80 amino acid residues long) presents a bias in its composition; it is enriched in charged amino acids, has a small number of hydrophobic residues, and has a high proportion of disorder-promoting residues. More precisely, CP12 is a conditionally disordered proteins (CDP) dependent upon the redox state of its four cysteine residues. During the day, reducing conditions prevail in the chloroplast, and CP12 is fully disordered. Under oxidizing conditions (night), its cysteine residues form two disulfide bridges that confer some stability to some structural elements. Like many CDPs, CP12 plays key roles, and its redox-dependent conditional disorder is important for the main function of CP12: the dark/light regulation of the Calvin-Benson-Bassham (CBB) cycle responsible for CO<sub>2</sub> assimilation. Oxidized CP12 binds to glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase and thereby inhibits their activity. However, recent studies reveal that CP12 may have other functions beyond the CBB cycle regulation. In this review, we report the discovery of this protein, its features as a disordered protein, and the many functions this small protein can have.https://www.mdpi.com/2218-273X/12/8/1047Calvin-Benson-Bassham cycleconditionally disordered proteinhistory of modern sciencemetabolism regulationmoonlighting proteinprotein-protein interaction |
| spellingShingle | Cassy Gérard Frédéric Carrière Véronique Receveur-Bréchot Hélène Launay Brigitte Gontero A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12 Biomolecules Calvin-Benson-Bassham cycle conditionally disordered protein history of modern science metabolism regulation moonlighting protein protein-protein interaction |
| title | A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12 |
| title_full | A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12 |
| title_fullStr | A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12 |
| title_full_unstemmed | A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12 |
| title_short | A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12 |
| title_sort | trajectory of discovery metabolic regulation by the conditionally disordered chloroplast protein cp12 |
| topic | Calvin-Benson-Bassham cycle conditionally disordered protein history of modern science metabolism regulation moonlighting protein protein-protein interaction |
| url | https://www.mdpi.com/2218-273X/12/8/1047 |
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