Evolution of permease diversity and energy-coupling mechanisms with special reference to the bacterial phosphotransferase system.
Biochim Biophys Acta
; 1018(2-3): 248-51, 1990 Jul 25.
Article
em En
| MEDLINE
| ID: mdl-2168212
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Membrana Transportadoras
/
Fosfotransferases
/
Escherichia coli
Idioma:
En
Ano de publicação:
1990
Tipo de documento:
Article