The ammonia channel protein AmtB from Escherichia coli is a polytopic membrane protein with a cleavable signal peptide

FEMS Microbiology Letters
J ThorntonMike Merrick

Abstract

The Escherichia coli ammonia channel protein, AmtB, is a homotrimeric polytopic inner membrane protein in which each subunit has 11 transmembrane helices. We have shown that the structural gene amtB encodes a preprotein with a signal peptide that is cleaved off to produce a topology with the N-terminus in the periplasm and the C-terminus in the cytoplasm. Deletion of the signal peptide coding region results in significantly lower levels of AmtB accumulation in the membrane but modification of the signal peptidase cleavage site, leading to aberrant cleavage, does not prevent trimer formation and does not inactivate the protein. The presence of a signal peptide is apparently not a conserved feature of all prokaryotic Amt proteins. Comparison of predicted AmtB sequences suggests that while Amt proteins in Gram-negative organisms utilize a signal peptide, the homologous proteins in Gram-positive organisms do not.

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Citations

Oct 8, 2009·Archives of Microbiology·Iris LükeFrank Sargent
Mar 11, 2009·Proceedings of the National Academy of Sciences of the United States of America·Raif Musa-AzizWalter F Boron
Jul 20, 2010·The Journal of Biological Chemistry·Martha V RadchenkoMike Merrick
Jun 13, 2012·Microbiology and Molecular Biology Reviews : MMBR·Ross E DalbeyJan Maarten van Dijl
Jan 6, 2009·BMC Bioinformatics·Khar Heng Choo, Shoba Ranganathan
Jan 16, 2007·Proceedings of the National Academy of Sciences of the United States of America·Matthew J ConroyMike Merrick
Nov 23, 2007·Proceedings of the National Academy of Sciences of the United States of America·Domenico LupoFritz K Winkler
Mar 28, 2006·Transfusion clinique et biologique : journal de la Société française de transfusion sanguine·M MerrickP A Bullough
May 4, 2016·Médecine sciences : M/S·Mélanie Boeckstaens
Dec 4, 2013·Microbiology and Molecular Biology Reviews : MMBR·Wally C van HeeswijkFred C Boogerd

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