title: Evolution of permease diversity and energy-coupling mechanisms with special reference to the bacterial phosphotransferase system.
abstract: Different classes of apparently unrelated permeases couple different forms of energy to solute transport. While the energy coupling mechanisms utilized by the different permease classes are clearly distinct, it is proposed, based on structural comparisons, that many of these permeases possess transmembrane, hydrophobic domains which are evolutionarily related. Carriers may have arisen from transmembrane pore-forming proteins, and the protein constituents or domains which are specifically responsible for energy coupling may have had distinct origins. Thus, complex permeases may possess mosaic structures. This suggestion is substantiated by recent findings regarding the evolutionary origins of the bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS). Mechanistic implications of this proposal are presented.
authors.affiliation: Department of Biology, University of California, San Diego, La Jolla 92093.
authors.forename: M H
authors.initials: MH
authors.lastname: Saier
authors.forename: L F
authors.initials: LF
authors.lastname: Wu
authors.forename: M E
authors.initials: ME
authors.lastname: Baker
authors.forename: G
authors.initials: G
authors.lastname: Sweet
authors.forename: A
authors.initials: A
authors.lastname: Reizer
authors.forename: J
authors.initials: J
authors.lastname: Reizer
mesh_terms: D005075:Biological Evolution; D004926:Escherichia coli / Q000201:enzymology*; D026901:Membrane Transport Proteins / Q000145:classification*; D010770:Phosphotransferases / Q000145:classification*
chemical_list: D026901:Membrane Transport Proteins; D010770:Phosphotransferases