Effects of the Terminal Regions on Rubisco Activase Form and Function
Thesis DisciplineBiological Sciences
Degree GrantorUniversity of Canterbury
Degree NameMaster of Science
Rubisco is the sole enzyme responsible for the incorporation of CO2 into sugar molecules useable by all life on earth. In the vast majority of discovered autotrophic organisms their respective rubisco has been accompanied by another enzyme called rubisco activase. The catalytically inefficient nature of rubisco requires rubisco activase yet much of its important activity remains undiscovered. Rubisco activase has at both of its terminal ends a dynamic and flexible domain that have poorly understood functional consequences. This projects aims are to gain a better understanding on how these terminal domains are required for rubisco activase. Various rubisco activase constructs were recombinantly purified and experimented on. The experiments included various kinetic assays and thermal melt temperatures but also powerful techniques such as analytical ultracentrifugation and small angle Xray scattering. The results show that the rubisco activase enzyme produces dynamic changes to its assembly and function with the binding of nucleotide and the addition and subtraction of terminal components.