Publications by authors named "Fiona J Woodger"

Cyanobacteria have evolved a significant environmental adaptation, known as a CO(2)-concentrating-mechanism (CCM), that vastly improves photosynthetic performance and survival under limiting CO(2) concentrations. The CCM functions to transport and accumulate inorganic carbon actively (Ci; HCO(3)(-), and CO(2)) within the cell where the Ci pool is utilized to provide elevated CO(2) concentrations around the primary CO(2)-fixing enzyme, ribulose bisphosphate carboxylase-oxygenase (Rubisco). In cyanobacteria, Rubisco is encapsulated in unique micro-compartments known as carboxysomes.

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Cyanobacterial photosynthesis occurs in radically diverse habitats and utilizes various forms of a CO(2)-concentrating mechanism (CCM) featuring multiple inorganic carbon (C(i)) transporters. Cyanobacteria from dynamic environments can transform CCM activity depending on C(i) availability, and yet the molecular basis for this regulation is unclear, especially in coastal strains. LysR family transcription factors resembling the Calvin cycle regulator CbbR from proteobacteria have been implicated in the expression of C(i) transporter genes in freshwater cyanobacteria.

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In most cyanobacteria, the gene rbcX is co-transcribed with the rbcL and rbcS genes that code for the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Previous co-expression studies in Escherichia coli of cyanobacterial Rubisco and RbcX have identified a chaperonin-like function for RbcX. The organization of the rbcLXS operon has, to a certain extent, precluded definitive gene function studies of rbcX in cyanobacteria.

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Freshwater cyanobacteria are subjected to large seasonal fluctuations in the availability of nutrients, including inorganic carbon (Ci). We are interested in the regulation of the CO2-concentrating mechanism (CCM) in the model freshwater cyanobacterium Synechococcus sp. strain PCC7942 in response to Ci limitation; however, the nature of Ci sensing is poorly understood.

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Cyanobacteria probably exhibit the widest range of diversity in growth habitats of all photosynthetic organisms. They are found in cold and hot, alkaline and acidic, marine, freshwater, saline, terrestrial, and symbiotic environments. In addition to this, they originated on earth at least 2.

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Cyanobacteria possess a highly effective CO(2)-concentrating mechanism that elevates CO(2) concentrations around the primary carboxylase, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). This CO(2)-concentrating mechanism incorporates light-dependent, active uptake systems for CO(2) and HCO(-)(3). Through mutant studies in a coastal marine cyanobacterium, Synechococcus sp.

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GAMYB is a GA-responsive activator of hydrolase gene expression in the aleurone layer of germinated cereal grains. We have isolated a putative GAMYB-binding protein, GMPOZ, which contains a BTB/POZ domain found in certain animal transcriptional regulators. Although BTB/POZ domain proteins are numerous in plants, very few are yet characterized.

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The cyanobacterial CO2-concentrating mechanism (CCM) allows photosynthesis to proceed in CO2-limited aquatic environments, and its activity is modulated in response to inorganic carbon (Ci) availability. Real-time reverse transcriptase-PCR analysis was used to examine the transcriptional regulation of more than 30 CCM-related genes in Synechococcus sp. strain PCC7942 with an emphasis on genes encoding high-affinity Ci transporters and carboxysome-associated proteins.

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GAMYB is a gibberellin (GA)-regulated activator of hydrolase gene expression in the aleurone layer of germinating cereal grains. Although it is clear that GAMYB expression is regulated by GA, more remains to be understood about how this transcription factor operates within the GA-response pathway. In order to isolate new components from the GA-response pathway, barley aleurone libraries were screened for GAMYB-binding proteins using a recently developed yeast two-hybrid system, which is compatible with the use of transcription factors as baits.

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