Characterization of the heterooligomeric red-type rubisco activase from red algae
The key photosynthetic CO2 fixing enzyme Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is prone to be inhibited by its own substrate RuBP and other sugar phosphates. In diverse organisms, various molecular chaperones termed the Rubisco activases have been recruited to remodel inhibited R...
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| Muut tekijät: | |
| Aineistotyyppi: | Opinnäyte |
| Kieli: | English |
| Julkaistu: |
2017
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| Aiheet: | |
| Linkit: | http://hdl.handle.net/10356/69463 |
| _version_ | 1826129413786304512 |
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| author | Loganathan, Nitin |
| author2 | Oliver Mueller-Cajar |
| author_facet | Oliver Mueller-Cajar Loganathan, Nitin |
| author_sort | Loganathan, Nitin |
| collection | NTU |
| description | The key photosynthetic CO2 fixing enzyme Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is prone to be inhibited by its own substrate RuBP and other sugar phosphates. In diverse organisms, various molecular chaperones termed the Rubisco activases have been recruited to remodel inhibited Rubisco complexes leading to the release of the inhibitors. Although red-type Rubiscos are a potential target in plant biotechnology to enhancing photosynthetic efficiency, their regulation is poorly studied. Here we biochemically characterized the two red-type Rubisco activase isoforms encoded by the thermophilic red algae Cyanidioschyzon merolae, as well as a homologue found in α-cyanobacteria. The individual algal isoforms are inactive in isolation, but when mixed form a functional hetero-oligomeric activase. Mutagenesis of key functional motifs indicates that ATP hydrolysis of the subunits is highly coordinated and that the nuclear-genome encoded isoform is more critical for activase function than the plastid-genome encoded counterpart. Our findings also suggest broad substrate compatibility among red-type Rubisco activases. |
| first_indexed | 2024-10-01T07:40:11Z |
| format | Thesis |
| id | ntu-10356/69463 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:40:11Z |
| publishDate | 2017 |
| record_format | dspace |
| spelling | ntu-10356/694632023-02-28T18:47:27Z Characterization of the heterooligomeric red-type rubisco activase from red algae Loganathan, Nitin Oliver Mueller-Cajar School of Biological Sciences DRNTU::Science::Biological sciences::Biochemistry The key photosynthetic CO2 fixing enzyme Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) is prone to be inhibited by its own substrate RuBP and other sugar phosphates. In diverse organisms, various molecular chaperones termed the Rubisco activases have been recruited to remodel inhibited Rubisco complexes leading to the release of the inhibitors. Although red-type Rubiscos are a potential target in plant biotechnology to enhancing photosynthetic efficiency, their regulation is poorly studied. Here we biochemically characterized the two red-type Rubisco activase isoforms encoded by the thermophilic red algae Cyanidioschyzon merolae, as well as a homologue found in α-cyanobacteria. The individual algal isoforms are inactive in isolation, but when mixed form a functional hetero-oligomeric activase. Mutagenesis of key functional motifs indicates that ATP hydrolysis of the subunits is highly coordinated and that the nuclear-genome encoded isoform is more critical for activase function than the plastid-genome encoded counterpart. Our findings also suggest broad substrate compatibility among red-type Rubisco activases. Doctor of Philosophy (SBS) 2017-01-24T07:39:42Z 2017-01-24T07:39:42Z 2017 Thesis Loganathan, N. (2017). Characterization of the heterooligomeric red-type rubisco activase from red algae. Doctoral thesis, Nanyang Technological University, Singapore. http://hdl.handle.net/10356/69463 10.32657/10356/69463 en 289 p. application/pdf |
| spellingShingle | DRNTU::Science::Biological sciences::Biochemistry Loganathan, Nitin Characterization of the heterooligomeric red-type rubisco activase from red algae |
| title | Characterization of the heterooligomeric red-type rubisco activase from red algae |
| title_full | Characterization of the heterooligomeric red-type rubisco activase from red algae |
| title_fullStr | Characterization of the heterooligomeric red-type rubisco activase from red algae |
| title_full_unstemmed | Characterization of the heterooligomeric red-type rubisco activase from red algae |
| title_short | Characterization of the heterooligomeric red-type rubisco activase from red algae |
| title_sort | characterization of the heterooligomeric red type rubisco activase from red algae |
| topic | DRNTU::Science::Biological sciences::Biochemistry |
| url | http://hdl.handle.net/10356/69463 |
| work_keys_str_mv | AT loganathannitin characterizationoftheheterooligomericredtyperubiscoactivasefromredalgae |