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His work in Geneva contributed to the discovery that RNase E, which is an essential endo-ribonuclease in E. coli, is a key enzyme in the initiation of mRNA degradation. In subsequent work, his group showed that RNase E is part of a large multienzyme RNA-degrading complex, which is now known as the RNA degradosome. Other work includes studies on the role of RhlB, PNPase and poly(A) polymerase in mRNA degradation, and identification of beta-CASP ribonucleases in the Archaea. His current research is based on the recent discovery that the RNA degradosome is localized to the inner cytoplasmic membrane of E. coli. His group characterized a conserved element in the non-catalytic region of RNase E that directly anchors the RNA degradosome to the phospholipid bilayer. They are now addressing the question of how association of the RNA degradosome with the inner membrane impacts RNA processing and degradation.
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biorxiv(2022)
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