PMID: 2120191Oct 1, 1990Paper

Involvement of the histidine protein (HPr) of the phosphotransferase system in chemotactic signaling of Escherichia coli K-12

Journal of Bacteriology
G GrüblJ W Lengeler

Abstract

It is known that in mutants of Escherichia coli lacking the histidine protein (HPr) of the carbohydrate: phosphotransferase system, all substrates of the system can be taken up in the presence of the fructose-regulated HPr-like protein FPr (gene fruF). Although this protein fully substituted for HPr in transport and phosphorylation, we found that it was not able to complement efficiently for HPr in mediating chemotaxis toward phosphotransferase system substrates. Furthermore, transport activity and chemotaxis could be genetically dissected by the exchange of single amino acids in HPr. The results suggest a specific role of HPr in chemotactic signaling. We propose a possible link of signal transduction pathways for phosphotransferase system- and methyl chemotaxis protein-dependent substrates via HPr.

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Citations

Jul 1, 1995·FEMS Microbiology Reviews·K J HellingwerfH V Westerhoff
Jan 1, 1993·Journal of Cellular Biochemistry·F Titgemeyer
Feb 19, 1998·Microbiology·Yehudit Jeziore-SassoonJudith P Armitage
Mar 6, 1999·Microbiology and Molecular Biology Reviews : MMBR·L L Madison, G W Huisman
Mar 1, 1992·Microbiological Reviews·J L Botsford, J G Harman
Sep 1, 1993·Microbiological Reviews·P W PostmaG R Jacobson
Dec 1, 1993·Microbiological Reviews·M Riley

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