Heterologous expression of a histone-like protein fromStreptococcus intermediusinEscherichia colialters the nucleoid structure and inhibits the growth ofE. coli

Abstract

Escherichia coli failed to survive after transformation with a Streptococcus intermedius histone-like protein gene (Si-hlp) and its promoter-harbored plasmid. The promoter function of Si-hlp in E. coli was determined using enhanced green fluorescence protein (egfp) gene as a reporter. The inhibitory effect of Si-HLP on E. coli viability was verified by a tetracycline-inducible gene expression system. Further study suggested that Si-HLP may alter the bacterial nucleoid structure, leading to the growth inhibition of E. coli.

Recombinant tagging system using ribosomal frameshifting to monitor protein expression

“…In particular, green fluorescent protein (GFP) from jellyfish is a versatile fluorescent protein marker, because it does not require additional cofactors or substrates (Chalfie et al, 1994). Since the GFP fluorescence signal is correlated to protein concentration, GFP can be used as a quantitative tool for real time identification of gene expression Kottmeier et al, 2011;Kuhn et al, 2010;Liu et al, 2008;Ribeiro-dos-Santos et al, 2010;Zhang and Yang, 2006). Since the GFP fluorescence signal is correlated to protein concentration, GFP can be used as a quantitative tool for real time identification of gene expression Kottmeier et al, 2011;Kuhn et al, 2010;Liu et al, 2008;Ribeiro-dos-Santos et al, 2010;Zhang and Yang, 2006).…”

“…A fusion protein of target and GFP proteins can be expressed in cells or organisms, and GFP fusion tags allow direct visualization of a target protein during dynamic cellular events (Bastiaens and Pepperkok, 2000;Lippincott-Schwartz et al, 2001). Since the GFP fluorescence signal is correlated to protein concentration, GFP can be used as a quantitative tool for real time identification of gene expression Kottmeier et al, 2011;Kuhn et al, 2010;Liu et al, 2008;Ribeiro-dos-Santos et al, 2010;Zhang and Yang, 2006). In many studies, the target protein was expressed only as fusions with GFP (March et al, 2003); multiple genes were fused in tandem to improve the yield of the target protein (Wu et al, 2001).…”