Genomics-guided approaches to enzyme discovery in disparate Galdieria species
Lead Research Organisation:
University of York
Department Name: Biology
Abstract
Galdieria is a red alga that displays enormous capacity to thrive at highly acidic conditions and elevated temperatures. It
displays broad metabolic repertoires allowing vigorous growth on virtually any carbon source. Galdieria is a metabolic
workhorse. Understanding the metabolic capacity of Galdieria under differing growth conditions assesses the biofuel,
antioxidant and materials-chemistry potential for this organism. This application is to discover Galdieria enzymes that
work in the bioconversion of untreated lignocellulosic biomass for bioenergy production of liquid fuels. We wish to use
the reference genome to facilitate transcriptomics and proteomics to guide enzyme discovery.
In phase 1 a genomics examination will be performed of induced transcripts as a result of numerous, differing
carbohydrate-media compositions of differing clades of Galdieria discovered through phylogenomic identification. These
growth-media sources include soluble carbohydrate and sugar-alcohol mixtures and complex insoluble residues such
as starch and wheat straw. This generates data sets to reveal novel lignocellulosic degradation enzymes in Galdieria.
The RNAs would be quantified and comparisons to the control would be performed to find those genes induced in
expression that can be annotated as catabolic enzymes. The list of annotated enzymes would be correlated from
compared tests to associate the transcriptomics compared to the Galdieria genome. Together a list of genes would be
complied for future exploration of encoded activity.
In phase 2 a proteomics survey would be performed of enzymes from Galdieria. Fractions of Galdieria strains grown on
complex wastes would be applied to mass spectroscopy. The identification of resultant peptides guides further
annotation. These proteins identified will be compared to the induced RNAs. In total a comprehensive list of proteins will
be unified from the genome to the transcriptome to the excreted proteome and this serves enzymology of recombinant
forms of such acid and heat stable proteins.
displays broad metabolic repertoires allowing vigorous growth on virtually any carbon source. Galdieria is a metabolic
workhorse. Understanding the metabolic capacity of Galdieria under differing growth conditions assesses the biofuel,
antioxidant and materials-chemistry potential for this organism. This application is to discover Galdieria enzymes that
work in the bioconversion of untreated lignocellulosic biomass for bioenergy production of liquid fuels. We wish to use
the reference genome to facilitate transcriptomics and proteomics to guide enzyme discovery.
In phase 1 a genomics examination will be performed of induced transcripts as a result of numerous, differing
carbohydrate-media compositions of differing clades of Galdieria discovered through phylogenomic identification. These
growth-media sources include soluble carbohydrate and sugar-alcohol mixtures and complex insoluble residues such
as starch and wheat straw. This generates data sets to reveal novel lignocellulosic degradation enzymes in Galdieria.
The RNAs would be quantified and comparisons to the control would be performed to find those genes induced in
expression that can be annotated as catabolic enzymes. The list of annotated enzymes would be correlated from
compared tests to associate the transcriptomics compared to the Galdieria genome. Together a list of genes would be
complied for future exploration of encoded activity.
In phase 2 a proteomics survey would be performed of enzymes from Galdieria. Fractions of Galdieria strains grown on
complex wastes would be applied to mass spectroscopy. The identification of resultant peptides guides further
annotation. These proteins identified will be compared to the induced RNAs. In total a comprehensive list of proteins will
be unified from the genome to the transcriptome to the excreted proteome and this serves enzymology of recombinant
forms of such acid and heat stable proteins.