| Autor: |
Gwin CM; 1Department of Biology, Hofstra University, Hempstead, NY, USA.; 2Department of Microbial Pathogenesis, Yale University, New Haven, CT, USA., Prakash N; 1Department of Biology, Hofstra University, Hempstead, NY, USA., Christian Belisario J; 3Department of Biomedical Sciences, College of Osteopathic Medicine, New York Institute of Technology, Old Westbury, NY, USA., Haider L; 1Department of Biology, Hofstra University, Hempstead, NY, USA.; 4College of Medicine, SUNY-Downstate Medical Center, Brooklyn, NY, USA., Rosen ML; 1Department of Biology, Hofstra University, Hempstead, NY, USA., Martinez LR; 3Department of Biomedical Sciences, College of Osteopathic Medicine, New York Institute of Technology, Old Westbury, NY, USA.; 5Department of Biological Sciences, The Border Biomedical Research Center, University of Texas at El Paso, El Paso, TX, USA., Rigel NW; 1Department of Biology, Hofstra University, Hempstead, NY, USA. |
| Abstrakt: |
Directing the flow of protein traffic is a critical task faced by all cellular organisms. In Gram-negative bacteria, this traffic includes lipoproteins. Lipoproteins are synthesized as precursors in the cytoplasm and receive their acyl modifications upon export across the inner membrane. The third and final acyl chain is added by Lnt, which until recently was thought to be essential in all Gram-negatives. In this report, we show that Acinetobacter species can also tolerate a complete loss-of-function mutation in lnt. Absence of a fully functional Lnt impairs modification of lipoproteins, increases outer membrane permeability and susceptibility to antibiotics, and alters normal cellular morphology. In addition, we show that loss of lnt triggers a global transcriptional response to this added cellular stress. Taken together, our findings provide new insights on and support the growing revisions to the Gram-negative lipoprotein biogenesis paradigm. |
