Genetic studies in Escherichia coli have implicated the unphosphorylated version of PtsN (unphospho-PtsN), the terminal phospho-acceptor of the PtsP-PtsO-PtsN phosphorelay, as a negative regulator of potassium (K) efflux mediated by YcgO. YcgO is a protein belonging to the CPA1 family of monovalent cation/proton antiporters. Here we show that in vivo, YcgO comprises an approximately 383 amino acid N-terminal transmembrane domain (TMD) and a 195 amino acid C-terminal cytoplasmic region (CTR).
View Article and Find Full Text PDFIn E. coli K-12, the absence of unphosphorylated PtsN (unphospho-PtsN) has been proposed to cause an L-leucine-sensitive growth phenotype (Leu) by hyperactivated K uptake mediated impairment of the expression of the ilvBN operon, encoding subunits of the L-valine (Val)-sensitive acetohydroxyacid synthase I (AHAS I) that renders residual AHAS activity susceptible to inhibition by Leu and K. This leads to AHAS insufficiency and a requirement for L-isoleucine (Ile).
View Article and Find Full Text PDF