Glycine-rich RNA binding protein of Oryza sativa inhibits growth of M15 E. coli cells

<p>Abstract</p> <p>Background</p> <p>Plant glycine-rich RNA binding proteins have been implicated to have roles in diverse abiotic stresses.</p> <p>Findings</p> <p><it>E. coli </it>M15 cells transformed with full-length rice glycine-rich RNA binding protein4 (OsGR-RBP4), truncated rice glycine-rich RNA binding protein4 (OsGR-RBP4ΔC) and rice FK506 binding protein (OsFKBP20) were analyzed for growth profiles using both broth and solid media. Expression of OsGR-RBP4 and OsGR-RBP4ΔC proteins caused specific, inhibitory effect on growth of recombinant M15 <it>E. coli </it>cells. The bacterial inhibition was shown to be time and incubation temperature dependent. Removal of the inducer, IPTG, resulted in re-growth of the cells, indicating that effect of the foreign proteins was of reversible nature. Although noted at different levels of dilution factors, addition of purified Os-GR-RBP4 and OsGR-RBP4ΔC showed a similar inhibitory effect as seen with expression inside the bacterial cells.</p> <p>Conclusions</p> <p>Expression of eukaryotic, stress-associated OsGR-RBP4 protein in prokaryotic <it>E. coli </it>M15 cells proves injurious to the growth of the bacterial cells. <it>E. coli </it>genome does not appear to encode for any protein that has significant homology to OsGR-RBP4 protein. Therefore, the mechanism of inhibition appears to be due to some illegitimate interactions of the OsGR-RBP4 with possibly the RNA species of the trans-host bacterial cells. The detailed mechanism underlying this inhibition remains to be worked out.</p

The role of parkin-picki in mithchondrial dysfunction

THESIS 9749Autosomal Recessive Juvenile Parkinsonism (ARJP) is the most common motor-related neurodegenerative disease, which occurs in young adults between 20-40 years of age. Mutations in the parkin (PARK2) gene are associated ARJP, which result in the loss of dopaminergic neurons of substantia nigra pars compacta in the mid brain. Parkin, an E3 ligase, is an enzyme responsible for ubiquitination of several proteins leading to their degradation in Ubiquitin Proteasomal System (UPS) and promoting autophagy of depolarized mitochondria. Mutations in the parkin gene are thought to result in protein aggregation of parkin substrates resulting in neuronal toxicity. Among these parkin interacting proteins and substrates, several play important roles in mitochondrial function, oxidative stress, cellular toxicity and apoptosis. This project focused on investigating the role of one particular protein that interacts with parkin, namely, PICK1. Specifically, the studies herein investigated the role of a parkin-PICK1 interaction in mitochondrial function and oxidative stress