Photosynthetica 2024, 62(1):90-101 | DOI: 10.32615/ps.2024.002
Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii
- 1 Department of Agricultural Biotechnology, Akdeniz University, 07058 Antalya, Turkey
- 2 Institute of Molecular Biology and Biotechnologies, Ministry of Science and Education, Republic of Azerbaijan, AZ 1073 Baku, Azerbaijan
Phosphoglycolate phosphatase (PGPase), a key enzyme in photosynthetic organisms, catalyzes the dephosphorylation of phosphoglycolate, which is largely produced by the oxygenase activity of Rubisco, and is a potent inhibitor of several Calvin cycle enzymes. PGPase (CrPGPase 1) was previously cloned, purified, and characterized from unicellular green Chlamydomonas reinhardtii. In silico analysis revealed two more candidates encoding PGPase enzymes in the C. reinhardtii genome. In this study, we isolated, cloned, and overexpressed three PGPase genes (pgp1, pgp2, pgp3) from C. reinhardtii and performed gene expression analysis at high and low ammonium [NH4+] concentrations. We demonstrate that all three pgp genes encode functionally active PGPases in C. reinhardtii. In addition, we show that pgp1 and pgp2 genes are N-responsive genes and are upregulated under low ammonium concentrations. In silico analysis revealed that PGPase exists mainly in three isoforms in higher plants and algae.
Additional key words: Chlamydomonas reinhardtii; gene expression; N-deficiency; phosphoglycolate; phosphoglycolate phosphatase; photorespiration.
Received: November 12, 2023; Revised: December 17, 2023; Accepted: January 8, 2024; Prepublished online: February 5, 2024; Published: February 22, 2024 Show citation
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