The apolipoprotein N-acyl transferase Lnt is dispensable for growth in Acinetobacter species
| Autor: | Lubaina Haider, J Christian Belisario, Luis R. Martinez, Nathan W. Rigel, Marlene L. Rosen, Celena M. Gwin, Natalia Prakash |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Cell Membrane Permeability Apolipoprotein B Acylation Lipoproteins 030106 microbiology Microbial Sensitivity Tests medicine.disease_cause Microbiology 03 medical and health sciences Bacterial Proteins Loss of Function Mutation medicine Inner membrane Mutation Microbial Viability Acinetobacter biology Chemistry Gene Expression Regulation Bacterial Anti-Bacterial Agents Cell biology Cytoplasm biology.protein Cell envelope Bacterial outer membrane Acyltransferases Biogenesis Research Article Lipoprotein |
| Zdroj: | Microbiology. 164:1547-1556 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/mic.0.000726 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|