Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii
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,...
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| Format: | Article |
| Language: | English |
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Academy of Sciences of the Czech Republic, Institute of Experimental Botany
2024-02-01
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| Series: | Photosynthetica |
| Subjects: | |
| Online Access: | https://ps.ueb.cas.cz/artkey/phs-202401-0010_isolation-cloning-and-gene-expression-analysis-of-phosphoglycolate-phosphatase-from-green-alga-chlamydomonas.php |
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| author | T. MAMEDOV G. ZAKIYEVA F. DEMIREL G. MAMMADOVA G. HASANOVA |
| author_facet | T. MAMEDOV G. ZAKIYEVA F. DEMIREL G. MAMMADOVA G. HASANOVA |
| author_sort | T. MAMEDOV |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-07T23:01:47Z |
| format | Article |
| id | doaj.art-0d957de272a7422a93de27e43fcb2b0d |
| institution | Directory Open Access Journal |
| issn | 0300-3604 1573-9058 |
| language | English |
| last_indexed | 2024-03-07T23:01:47Z |
| publishDate | 2024-02-01 |
| publisher | Academy of Sciences of the Czech Republic, Institute of Experimental Botany |
| record_format | Article |
| series | Photosynthetica |
| spelling | doaj.art-0d957de272a7422a93de27e43fcb2b0d2024-02-22T12:35:26ZengAcademy of Sciences of the Czech Republic, Institute of Experimental BotanyPhotosynthetica0300-36041573-90582024-02-016219010110.32615/ps.2024.002phs-202401-0010Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtiiT. MAMEDOV0G. ZAKIYEVA1F. DEMIREL2G. MAMMADOVA3G. HASANOVA4Department of Agricultural Biotechnology, Akdeniz University, 07058 Antalya, TurkeyInstitute of Molecular Biology and Biotechnologies, Ministry of Science and Education, Republic of Azerbaijan, AZ 1073 Baku, AzerbaijanDepartment of Agricultural Biotechnology, Akdeniz University, 07058 Antalya, TurkeyDepartment of Agricultural Biotechnology, Akdeniz University, 07058 Antalya, TurkeyDepartment of Agricultural Biotechnology, Akdeniz University, 07058 Antalya, TurkeyPhosphoglycolate 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.https://ps.ueb.cas.cz/artkey/phs-202401-0010_isolation-cloning-and-gene-expression-analysis-of-phosphoglycolate-phosphatase-from-green-alga-chlamydomonas.phpchlamydomonas reinhardtiigene expressionn-deficiencyphosphoglycolatephosphoglycolate phosphatasephotorespiration |
| spellingShingle | T. MAMEDOV G. ZAKIYEVA F. DEMIREL G. MAMMADOVA G. HASANOVA Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii Photosynthetica chlamydomonas reinhardtii gene expression n-deficiency phosphoglycolate phosphoglycolate phosphatase photorespiration |
| title | Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii |
| title_full | Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii |
| title_fullStr | Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii |
| title_full_unstemmed | Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii |
| title_short | Isolation, cloning, and gene expression analysis of phosphoglycolate phosphatase from green alga Chlamydomonas reinhardtii |
| title_sort | isolation cloning and gene expression analysis of phosphoglycolate phosphatase from green alga chlamydomonas reinhardtii |
| topic | chlamydomonas reinhardtii gene expression n-deficiency phosphoglycolate phosphoglycolate phosphatase photorespiration |
| url | https://ps.ueb.cas.cz/artkey/phs-202401-0010_isolation-cloning-and-gene-expression-analysis-of-phosphoglycolate-phosphatase-from-green-alga-chlamydomonas.php |
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