par Pottier, M.;Gilis, Dimitri 
;Boutry, M
Référence Trends in plant science, 23, 5, page (382-392)
Publication Publié, 2018-05-01
;Boutry, MRéférence Trends in plant science, 23, 5, page (382-392)
Publication Publié, 2018-05-01
Article révisé par les pairs
| Résumé : | 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. |
