Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubsico) activase
(RCase) facilitates activation of and the maintenance of Rubisco
activity by using ATP hydrolysis to release tightly bound sugar
phosphates from the catalytic sites of Rubisco.
Tobacco (N. tabacum) RCase is known for being heat stable,
thus the chimeric protein was created to confer thermostability to
the protein. A domain consisting of residues 267-334 in tobacco
RCase were replaced by the corresponding Arabidopsis domain.
Previously, overexpression of this chimeric protein promoted better
growth and higher rates of photosynthesis under high temperatures.
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