Membrane Localization of the RNase E - GFP fusion protein in E. coli
The metabolism of RNA in prokaryotes involves a number of processes including the degradation of mRNA, the post-transcriptional modification of RNA and the assembly of ribonucleoprotein complexes. E. coli was the first organism in which the mechanism of mRNA degradation was elucidated. Our research is focused on RNase E, a conserved endoribonuclease in Gram-negative bacteria, which is part of a large macromolecular complex known as the RNA degradosome. RNase E is at the center of a network of posttranscriptional control of gene expression involving RNA binding proteins and noncoding RNAs that affect translation initiation and mRNA degradation. In 2008, we showed that RNase E is localized at the periphery of the cell and bound to the inner cytoplasmic membrane. Our group currently explores the physiological role of RNase E compartmentalization using complementary approaches. We also study the evolution of RNase E and its protein partners throughout the bacterial kingdom.
Organisms studied :
Ribonucleases; RNA processing and decay; Post-transcriptional control of gene expression; Regulatory non-coding RNA; Molecular machineries; Spatial and temporal organization of the cell;