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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.

Original publication

DOI

10.1016/j.jmb.2004.05.046

Type

Journal article

Journal

J Mol Biol

Publication Date

23/07/2004

Volume

340

Pages

965 - 979

Keywords

Amino Acid Sequence, Binding Sites, Circular Dichroism, Endoribonucleases, Escherichia coli, Molecular Sequence Data, Multienzyme Complexes, Phosphopyruvate Hydratase, Polyribonucleotide Nucleotidyltransferase, Protein Binding, Protein Structure, Tertiary, RNA Helicases, RNA, Bacterial, RNA-Binding Proteins, Spectrometry, Mass, Electrospray Ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization