An Insight of RuBisCO Evolution through a Multilevel Approach
RuBisCO is the most abundant enzyme on earth; it regulates the organic carbon cycle in the biosphere. Studying its structural evolution will help to develop new strategies of genetic improvement in order to increase food production and mitigate CO<sub>2</sub> emissions. In the present wo...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-11-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/11/12/1761 |
| _version_ | 1827673919260196864 |
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| author | Vladimir Camel Gaston Zolla |
| author_facet | Vladimir Camel Gaston Zolla |
| author_sort | Vladimir Camel |
| collection | DOAJ |
| description | RuBisCO is the most abundant enzyme on earth; it regulates the organic carbon cycle in the biosphere. Studying its structural evolution will help to develop new strategies of genetic improvement in order to increase food production and mitigate CO<sub>2</sub> emissions. In the present work, we evaluate how the evolution of sequence and structure among isoforms I, II and III of RuBisCO defines their intrinsic flexibility and residue-residue interactions. To do this, we used a multilevel approach based on phylogenetic inferences, multiple sequence alignment, normal mode analysis, and molecular dynamics. Our results show that the three isoforms exhibit greater fluctuation in the loop between αB and βC, and also present a positive correlation with loop 6, an important region for enzymatic activity because it regulates RuBisCO conformational states. Likewise, an increase in the flexibility of the loop structure between αB and βC, as well as Lys330 (form II) and Lys322 (form III) of loop 6, is important to increase photosynthetic efficiency. Thus, the cross-correlation dynamics analysis showed changes in the direction of movement of the secondary structures in the three isoforms. Finally, key amino acid residues related to the flexibility of the RuBisCO structure were indicated, providing important information for its enzymatic engineering. |
| first_indexed | 2024-03-10T04:33:26Z |
| format | Article |
| id | doaj.art-1ad7b1963aad401f9654ffd8bcb08e10 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T04:33:26Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-1ad7b1963aad401f9654ffd8bcb08e102023-11-23T03:58:44ZengMDPI AGBiomolecules2218-273X2021-11-011112176110.3390/biom11121761An Insight of RuBisCO Evolution through a Multilevel ApproachVladimir Camel0Gaston Zolla1Grupo de Investigacion en Mutaciones & Biotecnología Vegetal, Facultad de Agronomía, Universidad Nacional Agraria La Molina, Av. La Molina s/n., Lima 12175, PeruGrupo de Investigacion en Mutaciones & Biotecnología Vegetal, Facultad de Agronomía, Universidad Nacional Agraria La Molina, Av. La Molina s/n., Lima 12175, PeruRuBisCO is the most abundant enzyme on earth; it regulates the organic carbon cycle in the biosphere. Studying its structural evolution will help to develop new strategies of genetic improvement in order to increase food production and mitigate CO<sub>2</sub> emissions. In the present work, we evaluate how the evolution of sequence and structure among isoforms I, II and III of RuBisCO defines their intrinsic flexibility and residue-residue interactions. To do this, we used a multilevel approach based on phylogenetic inferences, multiple sequence alignment, normal mode analysis, and molecular dynamics. Our results show that the three isoforms exhibit greater fluctuation in the loop between αB and βC, and also present a positive correlation with loop 6, an important region for enzymatic activity because it regulates RuBisCO conformational states. Likewise, an increase in the flexibility of the loop structure between αB and βC, as well as Lys330 (form II) and Lys322 (form III) of loop 6, is important to increase photosynthetic efficiency. Thus, the cross-correlation dynamics analysis showed changes in the direction of movement of the secondary structures in the three isoforms. Finally, key amino acid residues related to the flexibility of the RuBisCO structure were indicated, providing important information for its enzymatic engineering.https://www.mdpi.com/2218-273X/11/12/1761Bio3Dstructural dynamicsstructural flexibilitycross-correlation dynamics |
| spellingShingle | Vladimir Camel Gaston Zolla An Insight of RuBisCO Evolution through a Multilevel Approach Biomolecules Bio3D structural dynamics structural flexibility cross-correlation dynamics |
| title | An Insight of RuBisCO Evolution through a Multilevel Approach |
| title_full | An Insight of RuBisCO Evolution through a Multilevel Approach |
| title_fullStr | An Insight of RuBisCO Evolution through a Multilevel Approach |
| title_full_unstemmed | An Insight of RuBisCO Evolution through a Multilevel Approach |
| title_short | An Insight of RuBisCO Evolution through a Multilevel Approach |
| title_sort | insight of rubisco evolution through a multilevel approach |
| topic | Bio3D structural dynamics structural flexibility cross-correlation dynamics |
| url | https://www.mdpi.com/2218-273X/11/12/1761 |
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