4.6 Article

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

Journal

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2007.05.223

Keywords

calcium channels; inclusion bodies; bacteria; polyhydroxybutyrate; aequorin; calcium in bacteria

Funding

  1. Wellcome Trust [075897] Funding Source: Medline

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The results here are the first clear demonstration of a physiological role for cytosolic Ca2+ in Escherichia coli by releasing a Ca2+ binding protein, apoaequorin, from inclusion bodies. In growth medium LB the cytosolic free Ca2+ was 0.1-0.3 mu M. Addition of EGTA reduced this to < 0.1 mu M, whereas addition of Ca2+ (10 mM) resulted in a cytosolic free Ca2+ of 1-2 mu M for at least 2 h. Ca2+ 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 Ca2+ was explained by release of protein from the inclusion bodies, together with a stabilisation of apoaequorin against degradation. Ca2+ also reduced the generation time by 4-5 min. These results have important implications for unravelling the physiological role of cytosolic Ca2+ in bacteria, particularly where several species are competing for the same nutrients, such as in the gut. (c) 2007 Published by Elsevier Inc.

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