An ffh mutant of Streptococcus mutans is viable and able to physiologically adapt to low pH in continuous culture

FEMS Microbiol Lett. 2004 May 15;234(2):315-24. doi: 10.1016/j.femsle.2004.03.043.

Abstract

Previously, we described in Streptococcus mutans strain NG8 a 5-gene operon (sat) that includes ffh, the bacterial homologue of the eukaryotic signal recognition particle (SRP) protein, SR54. A mutation in ffh resulted in acid sensitivity but not loss of viability. In the present study, chemostat-grown cells of the ffh mutant were shown to possess only 26% and 39% of the parental membrane F-ATPase activity and 55% and 75% of parental glucose-phosphotransferase (PTS) activity when pH-7 and pH-5-grown cells, respectively, were assayed. Two-dimensional-gel electrophoretic analyses revealed significant differences in protein profiles between parent and ffh-mutant strains at both pH 5 and pH 7. It appears that the loss of active SRP (Ffh) function, while not lethal, results in substantial alterations in cellular physiology that includes acid tolerance.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acclimatization
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Cell Membrane / physiology
  • Hydrogen-Ion Concentration*
  • Kinetics
  • Operon / genetics*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism*
  • Proton-Translocating ATPases / metabolism
  • Signal Recognition Particle / genetics
  • Signal Recognition Particle / metabolism
  • Streptococcus mutans / enzymology
  • Streptococcus mutans / genetics*
  • Streptococcus mutans / growth & development
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Signal Recognition Particle
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • Proton-Translocating ATPases