The Hidden Face of Rubisco
| Autor: | Dimitri Gilis, Mathieu Pottier, Marc Boutry |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0106 biological sciences 0301 basic medicine Oxygenase Protein Conformation Ribulose-Bisphosphate Carboxylase Protein subunit Plant Science Photosynthesis 01 natural sciences Gene Expression Regulation Enzymologic 03 medical and health sciences Gene Expression Regulation Plant Phylogeny Plant Proteins biology Phylum RuBisCO Metabolism Carbon Dioxide Plants Trichome Pyruvate carboxylase 030104 developmental biology Biochemistry biology.protein 010606 plant biology & botany |
| Zdroj: | Trends in Plant Science. 23:382-392 |
| ISSN: | 1360-1385 |
| DOI: | 10.1016/j.tplants.2018.02.006 |
| Popis: | Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) fixes atmospheric CO2 into organic compounds and is composed of eight copies each of a large subunit (RbcL) and a small subunit (RbcS). Recent reports have revealed unusual RbcS, which are expressed in particular tissues and confer higher catalytic rate, lesser affinity for CO2, and a more acidic profile of the activity versus pH. The resulting Rubisco was proposed to be adapted to a high CO2 environment and recycle CO2 generated by the metabolism. These RbcS belong to a cluster named T (for trichome), phylogenetically distant from cluster M, which gathers well-characterized RbcS expressed in mesophyll or bundle-sheath tissues. Cluster T is largely represented in different plant phyla, including pteridophytes and bryophytes, indicating an ancient origin. |
| Databáze: | OpenAIRE |
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