Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Nature 437

Abstract

The coordinated regulation of gene expression is required for homeostasis, growth and development in all organisms. Such coordination may be partly achieved at the level of messenger RNA stability 1 , in which the targeted destruction of subsets of transcripts generates the potential for cross-regulating metabolic pathways. In Escherichia coli, the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors E. coli RNase E is one of the largest members of a highly conserved RNase family The 'large' domain (residues 1-400) can be divided into subdomains corresponding to established folds ( The three RNAs that crystallized together with RNase E contain the targeted sequence 5 0 -ACAGUAUUUG-3 0 found at the 5 0 end of the antisense regulator of ColE1-type plasmid replication, RNA I 23 ( Whereas the 10-mer and 13-mer RNAs are bound entirely by one tetramer, the 15-mer RNA is long enough for it to be shared between two different tetramers in the crystal lattice The group on the 5 0 terminus of the RNA substrate can affect the catalytic rate constant of RNase E by orders of magnitude 12 but does not seem to have a marked effect on substrate bindin