Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E.

Journal article

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-te...

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Authors: Callaghan, A; Aurikko, J; Ilag, L; Günter Grossmann, J; Chandran, V

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 340
• Issue: 5
• Pages: 965-979
• Publication date: 2004-07-01
• DOI: 10.1016/j.jmb.2004.05.046
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: RNA, Bacterial; Circular Dichroism; Amino Acid Sequence; Escherichia coli; Phosphopyruvate Hydratase; Protein Structure, Tertiary; Polyribonucleotide Nucleotidyltransferase; RNA Helicases; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; RNA-Binding Proteins; Endoribonucleases; Binding Sites; Multienzyme Complexes; Protein Binding; Molecular Sequence Data; Spectrometry, Mass, Electrospray Ionization