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

Naseem, Riffat, Rosser-Davies, Sally J., Jones, Helen, Wann, Kenneth Taylor, Holland, Barry and Campbell, Anthony Keith 2007. Cytosolic Ca2+ regulates protein expression in E. coli through release from inclusion bodies. Biochemical and Biophysical Research Communications 360 (1) , pp. 33-39. 10.1016/j.bbrc.2007.05.223

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Abstract

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 ?M. Addition of EGTA reduced this to <0.1 ?M, whereas addition of Ca2+ (10 mM) resulted in a cytosolic free Ca2+ of 1–2 ?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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Pharmacy
Subjects: R Medicine > R Medicine (General)
Uncontrolled Keywords: Calcium channels ; Inclusion bodies ; Bacteria ; Polyhydroxybutyrate ; Aequorin ; Calcium in bacteria
ISSN: 1090-2104
Last Modified: 05 Jun 2017 01:39
URI: http://orca-mwe.cf.ac.uk/id/eprint/980

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