Examining Protein Translocation by ß-Barrel Membrane Proteins Using Reconstituted Proteoliposomes.
Methods Mol Biol
; 2778: 83-99, 2024.
Article
em En
| MEDLINE
| ID: mdl-38478273
ABSTRACT
ß-barrel membrane proteins populate the outer membrane of Gram-negative bacteria, mitochondria, and chloroplasts, playing significant roles in multiple key cellular pathways. Characterizing the functions of these membrane proteins in vivo is often challenging due to the complex protein network in the periplasm of Gram-negative bacteria (or intermembrane space in mitochondria and chloroplasts) and the presence of other outer membrane proteins. In vitro reconstitution into lipid-bilayer-like environments such as nanodiscs or proteoliposomes provides an excellent method for examining the specific function and mechanism of these membrane proteins in an isolated system. Here, we describe the methodologies employed to investigate Slam, a 14-stranded ß-barrel membrane protein also known as the type XI secretion system that is responsible for translocating proteins across the outer membrane of many bacterial species.
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Base de dados:
MEDLINE
Assunto principal:
Proteolipídeos
/
Proteínas da Membrana Bacteriana Externa
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article