The Erp protein is anchored at the surface by a carboxy-terminal hydrophobic domain and is important for cell-wall structure in Mycobacterium smegmatis.
Erp (Exported Repetitive Protein), also known as P36, Pirg and Rv3810, is a member of a mycobacteria-specific family of extracellular proteins. In pathogenic species, the erp gene has been described as a virulence factor. The Erp proteins comprise three domains. The N- and C-terminal domains are similar in all mycobacterial species, while the central domain consists of a repeated module that differs considerably between species. Here we show that the Erp protein is loosely attached to the surface and that the carboxy-terminal domain, which displays hydrophobic features, anchors Erp at the surface of the bacillus. The hydrophobic region is not necessary for the complementation of the altered colony morphology of a Mycobacterium smegmatis erp- mutant but proved to be necessary to achieve resistance to detergent at wild-type levels.
Unité de Génétique Mycobactérienne, Institut Pasteur, F-75724 Paris Cedex 15, France.
Dana
D
Kocíncová
Berit
B
Sondén
Leila
L
de Mendonça-Lima
Brigitte
B
Gicquel
Jean-Marc
JM
Reyrat
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002473:Cell Wall / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D003902:Detergents; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D020102:Mycobacterium smegmatis / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D012967:Sodium Dodecyl Sulfate
D001426:Bacterial Proteins; D003902:Detergents; C096737:ERP protein, Mycobacterium tuberculosis; D008565:Membrane Proteins; D012967:Sodium Dodecyl Sulfate