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  • Title: Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E.
    Author: Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF.
    Journal: J Mol Biol; 2004 Jul 23; 340(5):965-79. PubMed ID: 15236960.
    Abstract:
    The hydrolytic endoribonuclease RNase E, which is widely distributed in bacteria and plants, plays key roles in mRNA degradation and RNA processing in Escherichia coli. The enzymatic activity of RNase E is contained within the conserved amino-terminal half of the 118 kDa protein, and the carboxy-terminal half organizes the RNA degradosome, a multi-enzyme complex that degrades mRNA co-operatively and processes ribosomal and other RNA. The study described herein demonstrates that the carboxy-terminal domain of RNase E has little structure under native conditions and is unlikely to be extensively folded within the degradosome. However, three isolated segments of 10-40 residues, and a larger fourth segment of 80 residues, are predicted to be regions of increased structural propensity. The larger of these segments appears to be a protein-RNA interaction site while the other segments possibly correspond to sites of self-recognition and interaction with the other degradosome proteins. The carboxy-terminal domain of RNase E may thus act as a flexible tether of the degradosome components. The implications of these and other observations for the organization of the RNA degradosome are discussed.
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