Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

Abstract

Threading Through Protein antibiotics (bacteriocins) are frequently deployed by Gram-negative bacteria to combat competitors, a trait common in pathogens such as Escherichia coli, Yersinia pestis, Pseudomonas aeruginosa, Xanthomonas campestris , and Klebsiella pneumonia . As a result, bacteriocins are being developed as species-specific antibacterials. Bacteriocins must establish a translocon at the bacterial outer membrane in order to translocate into cells. Working in E. coli , Housden et al. (p. 1570 ) describe how the deoxyribonuclease, colicin E9, crosses the bacterial cell membrane by threading through a porin.