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

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Science  28 Jun 2013:
Vol. 340, Issue 6140, pp. 1570-1574
DOI: 10.1126/science.1237864

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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.