Biochemical and molecular analyses of the C-terminal domain of Era GTPase from Streptococcus pneumoniae

Article Abstract:

Evidence shows that the C-terminus of the Era protein, an essential GTPase, might be responsible for the binding of the protein to the cytoplasmic membrane and play a role in cellular function. This can be gleaned from an experiment in which an era gene from Streptococcus pneumoniae was identified and cloned and a mutant era gene with a deletion of 68 codons from its 3'-terminus was synthesized. Results show that the truncated Era protein, unlike the full-length Era protein, was not able to bind to the Escherichia coli cytoplasmic membrane.

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Era GTPase of Escherichia coli: binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates

Article Abstract:

Era, an essential GTPase, in Escherichia coli is discussed. Its binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates are of interest. Native Era, glutathione S transferase-fusion Era, His-tagged Era and proteins from E. coli have been expressed and purified. Native Era protein purified by a a 3- step column chromatographic method had lower GTPase activity vs that of GST-Era and His-Era proteins purified by 1-step affinity column chromatographic methods.

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Escherichia coli acid resistance: cAMP receptor protein and a 20 bp cis-acting sequence control pH and stationary phase expression of the gadA and gadBC glutamate decarboxylase genes

Article Abstract:

Research demonstrates that three proteins, gadA, gadB, and gadC, are associated with glutamate-dependent acid resistance in Escherichia coli. Results show that gadA and gadB glutamate decarboxylases utilize glutamic acid during pH 2 acid challenge.

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