Ribosome modulation factor protects Escherichia coli during heat stress, but this may not be dependent on ribosome dimerisation.
The role of ribosome modulation factor (RMF) in protecting heat-stressed Escherichia coli cells was identified by the observation that cultures of a mutant strain lacking functional RMF (HMY15) were highly heat sensitive in stationary phase compared to those of the parent strain (W3110). No difference in heat sensitivity was observed between these strains in exponential phase, during which RMF is not synthesised. Studies by differential scanning calorimetry demonstrated that the ribosomes of stationary-phase cultures of the mutant strain had lower thermal stability than those of the parent strain in stationary phase, or exponential-phase ribosomes. More rapid breakdown of ribosomes in the mutant strain during heating was confirmed by rRNA analysis and sucrose density gradient centrifugation. Analyses of ribosome composition showed that the 100S dimers dissociated more rapidly during heating than 70S particles. While ribosome dimerisation is a consequence of the conformational changes caused by RMF binding, it may not therefore be essential for RMF-mediated ribosome stabilisation.
Food Microbial Sciences Unit, School of Food Biosciences, The University of Reading, Whiteknights, P.O. Box 226, RG6 6AP, Reading, UK. g.w.niven@reading.ac.uk
Gordon W
GW
Niven
D001665:Binding Sites; D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D012269:Ribosomal Proteins / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D012270:Ribosomes / Q000502:physiology*
D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins; C063545:ribosome modulation factor, E coli