Secretins take shape.
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.
Molecular Genetics Unit and CNRS URA 2172, Institut Pasteur, 25, rue du Dr Roux, 75724 Paris CEDEX 15, France.
Nicolas
N
Bayan
Ingrid
I
Guilvout
Anthony P
AP
Pugsley
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D016941:Myxococcus xanthus / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008565:Membrane Proteins; C107109:Tgl protein, Myxococcus xanthus; C084295:pilQ protein, bacteria; D036781:Fimbriae Proteins