But this mutant clearly indicated that another factor was involved in the “light activation” of Rubisco. With Douglas Jordan : Meanwhile, Ogren and a graduate student, Douglas (Doug) Jordan, also initiated studies directed at understanding the biochemical factors that determine the specificity of the enzyme for CO2 versus oxygen. They developed a convenient method to accurately assay specificity and discovered that an order of magnitude variation in the enzyme’s specificity occurs naturally in diverse photosynthetic species (Jordan and Ogren 1981). They reasoned 4SC-202 cell line that this variation was an evolutionary response to the natural environment and geological changes
in
the composition of the atmosphere. In view of the global climate change, challenges remain high, but this research provides the basis for the continuing optimism in many labs throughout the world since P505-15 Rubisco can be modified to improve the photosynthetic efficiency of crop species through appropriate changes in enzyme structure. With Mike Salvucci and Archie Portis : The Arabidopsis mutant that Chris Sommerville had isolated languished in the lab for a few years. However, Ogren encouraged a new postdoc, Mike Salvucci and one of us (ARP)—still a relatively young hire, looking for an important research focus—in a renewed attack to identify what was exactly wrong with this mutant. In 1985 with some good fortune, Salvucci et al. (1985) were able to establish genetically, physiologically, and biochemically that the activity of Rubisco is regulated selleck compound by another protein, which was named Rubisco activase (Salvucci et al. 1985). The isolation and characterization of
the heretofore unsuspected Rubisco activase protein resolved several long-standing dilemmas regarding the regulation of Rubisco activity (see Portis 2003). Figure 5 shows a 1985 photograph of William Ogren and Michael Salvucci examining the protein gels which first demonstrated the physical Depsipeptide concentration existence of Rubisco activase. Two related Rubisco activase proteins were identified by comparing extracts of Arabidopsis wild-type and a Rubisco activase-deficient mutant (see Portis and Salvucci 2002). Fig. 5 A 1985 photograph of William Ogren (left) and Michael Salvucci examining the protein gels which first demonstrated the physical existence of Rubisco activase (see Portis and Salvucci 2002) With Jeff Werneke : Ogren and graduate student Werneke followed up these studies by taking advantage of recently developed molecular biology tools to isolate the gene and thereby discovering that the expression of the protein involves an alternative pre-mRNA splicing process (Werneke et al. 1989). This was the first characterization of such a process in a plant.