Topogenic signals in integral membrane proteins.
Eur J Biochem
; 174(4): 671-8, 1988 Jul 01.
Article
en En
| MEDLINE
| ID: mdl-3134198
Integral membrane proteins are characterized by long apolar segments that cross the lipid bilayer. Polar domains flanking these apolar segments have a more balanced amino acid composition, typical for soluble proteins. We show that the apolar segments from three different kinds of membrane-assembly signals do not differ significantly in amino acid content, but that the inside/outside location of the polar domains correlates strongly with their content of arginyl and lysyl residues, not only for bacterial inner-membrane proteins, but also for eukaryotic.proteins from the endoplasmic reticulum, the plasma membrane, the inner mitochondrial membrane, and the chloroplast thylakoid membrane. A positive-inside rule thus seems to apply universally to all integral membrane proteins, with apolar regions targeting for membrane integration and charged residues providing the topological information.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Aminoácidos
/
Proteínas de la Membrana
Idioma:
En
Revista:
Eur J Biochem
Año:
1988
Tipo del documento:
Article
País de afiliación:
Suecia
Pais de publicación:
Reino Unido