ABSTRACT
A mutant defective in the enzyme RNase P was isolated by P. SCHEDL and P. PRIMAKOFF (1973). The mutation rnpA49 found in this strain, which confers temperature sensitivity on carrier strains, was mapped by conjugation and transduction experiments and located around minute 82 of the E . coli map, with the suggested order rnpA bglB phoS rbsP ilv. As expected, the rnpA49 mutation is recessive. Even though this mutation is conditional, it is manifested at temperatures at which the carrier strains can grow.
In Escherichia coli and many other bacterial species, the glycolytic enzyme enolase is a component of the multi-enzyme RNA degradosome, an assembly that is involved in RNA processing and degradation. Enolase is recruited into the degradosome through interactions with a small recognition motif located within the degradosome-scaffolding domain of RNase E. Here, the crystal structure of enolase bound to its cognate site from RNase E (residues 823–850) at 1.9 Å resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E.
The RNA Processing Enzyme Polynucleotide Phosphorylase Negatively Controls Biofi lm Formation by Repressing Poly-N-Acetylglucosamine (PNAG) Production in Escherichia coli C