Title: Export and assembly of outer membrane proteins in E. coli
Abstract: Publisher Summary The outer membrane of Escherichia coli is an extremely asymmetric bilayer containing phospholipids and lipopolysaccharides (LPS) only in the inner and outer monolayer, respectively. It protects the cell by forming a barrier for harmful compounds, such as bile salts and enzymes, and prevents periplasmic proteins leaking into the medium. The outer membrane also contains a number of proteins (OMPs). After their synthesis in the cytoplasm, OMPs have to pass through the inner membrane before reaching their destination. The fact that these proteins don't end up in the inner membrane suggests either that these proteins have a structure that is incompatible with stable insertion into this membrane or that they somehow bypass this membrane on their way out. This chapter introduces the leading characters in this process and discusses their structure within the outer membrane, because this is important to understand the assembly process. For the transport across the inner membrane, OMPs follow the same pathway as periplasmic proteins. This pathway is discussed with only some special attention to the role of SecB protein that is of special importance in the export of OMPs. The focus of this chapter is on the folding process of OMPs and on their insertion and assembly into the outer membrane.
Publication Year: 1995
Publication Date: 1995-01-01
Language: en
Type: book-chapter
Indexed In: ['crossref']
Access and Citation
Cited By Count: 3
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