Secretins take shape

• Published in: Molecular microbiology 2006-04, Vol.60 (1), p.1-4
• Main Authors: Bayan, Nicolas, Guilvout, Ingrid, Pugsley, Anthony P.
• Format: Article
• Language: English
• Subjects: Bacterial Outer Membrane Proteins; Bacterial Outer Membrane Proteins - genetics; Bacterial Outer Membrane Proteins - metabolism; Bacterial Proteins; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Cell culture; Fimbriae Proteins; Fimbriae, Bacterial; Fimbriae, Bacterial - metabolism; Life Sciences; Membrane Proteins; Membrane Proteins - genetics; Membrane Proteins - metabolism; Membranes; Molecular biology; Myxococcus xanthus; Myxococcus xanthus - genetics; Myxococcus xanthus - growth & development; Myxococcus xanthus - metabolism; Other
• ISSN: 0950-382X; 1365-2958
• DOI: 10.1111/j.1365-2958.2006.05084.x

Summary Secretins are a unique class of bacterial multimeric outer membrane proteins that probably differ considerably from other, less complex outer membrane proteins in their overall structure and organization, and in their requirements for outer membrane targeting and assembly factors. In this MicroCommentary, we discuss these differences with respect to the role of a specific class of lipoproteins, often referred to as pilotins, in secretin complex assembly. We compare them with other lipoproteins that play a role in Omp85/YaeT‐mediated assembly of more classical outer membrane proteins. One of the examples we have chosen is the Myxococcus Xanthus lipoprotein Tgl. Coculture of cells with and without Tgl allows secretin assembly (and, hence, type IV pilus assembly) in the cells without Tgl, indicating that it can act by cell‐to‐cell contact or can transfer between cells.