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Article Dans Une Revue Biochemical and Biophysical Research Communications Année : 2007

Cytosolic Ca2+ regulates protein expression in E. coli through release from inclusion bodies.

Riffat Naseem
  • Fonction : Auteur
Sally Rosser Davies
  • Fonction : Auteur
Helen Jones
  • Fonction : Auteur
Kenneth T Wann
  • Fonction : Auteur
Anthony K Campbell
  • Fonction : Auteur

Résumé

The results here are the first clear demonstration of a physiological role for cytosolic Ca(2+) in Escherichia coli by releasing a Ca(2+) binding protein, apoaequorin, from inclusion bodies. In growth medium LB the cytosolic free Ca(2+) was 0.1-0.3 microM. Addition of EGTA reduced this to <0.1 microM, whereas addition of Ca(2+) (10mM) resulted in a cytosolic free Ca(2+) of 1-2 microM for at least 2h. Ca(2+) caused a 1.5- to 2-fold increase in the level of apoaequorin induced by IPTG. Whereas EGTA induced a 50% decrease. The effect of a Ca(2+) was explained by release of protein from the inclusion bodies, together with a stabilisation of apoaequorin against degradation. Ca(2+) also reduced the generation time by 4-5 min. These results have important implications for unravelling the physiological role of cytosolic Ca(2+) in bacteria, particularly where several species are competing for the same nutrients, such as in the gut.

Dates et versions

hal-00195304 , version 1 (10-12-2007)

Identifiants

Citer

Riffat Naseem, Sally Rosser Davies, Helen Jones, Kenneth T Wann, I Barry Holland, et al.. Cytosolic Ca2+ regulates protein expression in E. coli through release from inclusion bodies.. Biochemical and Biophysical Research Communications, 2007, 360 (1), pp.33-9. ⟨10.1016/j.bbrc.2007.05.223⟩. ⟨hal-00195304⟩
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