Project description:This study uses iTRAQ based proteomics approach to understand the cellular metabolic machineries present within the Clostridium strain BOH3 (discovered by our group) which can simultaneously utilise both glucose (six carbon sugar) and xylose (five carbon sugar) to produce butanol and riboflavin.
Project description:To investigate the transcriptional changes occurred in astrocytes after inflammatory or hemorrhagic stroke in vitro, we performed RNA sequencing (RNA-seq) of resting-MCM treated astrocytes, LPS-MCM treated astrocytes, and Hemin-MCM treated astrocytes.
Project description:Dihydropyrimidine dehydrogenase (PydA) catalyzes the first step of the reductive pyrimidine degradation (Pyd) pathway in bacteria and eukaryotes, enabling pyrimidines to be utilized as substrates for growth. PydA homologs studied to date catalyze the reduction of uracil to dihydrouracil, coupled to the oxidation of NAD(P)H. Uracil reduction occurs at a flavin mononucleotide (FMN) site, and NAD(P)H oxidation occurs at a flavin adenine dinucleotide (FAD) site, with two ferredoxin domains thought to mediate inter-site electron transfer. Here, we report the biochemical characterization of a Clostridial PydA homolog (PydAc) from a Pyd gene cluster in the strict anaerobic bacterium Clostridium chromiireducens. PydAc lacks the FAD domain, and instead is able to catalyze uracil reduction using reduced methyl viologen or reduced ferredoxin as the electron source. Homologs of PydAc are present in Pyd gene clusters in many strict anaerobic bacteria, which use reduced ferredoxin as an intermediate in their energy metabolism.