Loss of PII-dependent control of arginine biosynthesis in Dunaliella salina
Copyright © 2024 Elsevier B.V. All rights reserved.
| Veröffentlicht in: | Plant science : an international journal of experimental plant biology. - 1985. - 351(2024) vom: 23. Feb., Seite 112327 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2025
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| Zugriff auf das übergeordnete Werk: | Plant science : an international journal of experimental plant biology |
| Schlagworte: | Journal Article Arginine biosynthesis Dunaliella salina N-acetyl-L-glutamate kinase PII-signal proteins Salinity tolerance Arginine 94ZLA3W45F Phosphotransferases (Carboxyl Group Acceptor) EC 2.7.2.- mehr... |
| Zusammenfassung: | Copyright © 2024 Elsevier B.V. All rights reserved. In cyanobacteria and most Archaeplastida, Arg regulates its formation via allosteric inhibition of the controlling enzyme, N-acetyl-L-glutamate kinase (NAGK) that requires PII protein to properly sense the feedback inhibitor. Although PII expression has been shown to be reduced in Dunaliella salina compared to other green algae, the potential impact of this protein on DsNAGK activity remains unclear. We here performed coupled enzyme assay and surface plasmon resonance analysis and show that DsNAGK is activated by NAG and inhibited by Arg but is not controlled by DsPII. Moreover, DsPII has likely lost its function as an effective glutamine sensor. Replacement of the C-terminus from DsPII with the C-terminus from Chlamydomonas PII restored sensitivity to glutamine in a recombinant DsPII protein, demonstrating the importance of C-terminal residues close to the Q-loop for PII functions. The findings are discussed in the context of the relationship between NAGK control and the acquisition of salinity tolerance during evolution |
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| Beschreibung: | Date Completed 07.12.2024 Date Revised 07.12.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2259 |
| DOI: | 10.1016/j.plantsci.2024.112327 |