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A dynamin‐like protein involved in bacterial cell membrane surveillance under environmental stress
Author(s) -
Sawant Prachi,
Eissenberger Kristina,
Karier Laurence,
Mascher Thorsten,
Bramkamp Marc
Publication year - 2016
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.13110
Subject(s) - biology , microbiology and biotechnology , bacterial outer membrane , bacteria , bacillus subtilis , innate immune system , dynamin , membrane , bacterial cell structure , lipid bilayer , biophysics , immune system , cell , biochemistry , immunology , escherichia coli , genetics , endocytosis , gene
Summary In ever‐changing natural environments, bacteria are continuously challenged with numerous biotic and abiotic stresses. Accordingly, they have evolved both specific and more general mechanisms to counteract stress‐induced damage and ensure survival. In the soil habitat of B acillus subtilis , peptide antibiotics and bacteriophages are among the primary stressors that affect the integrity of the cytoplasmic membrane. Dynamin‐like proteins ( DLPs ) play a major role in eukaryotic membrane re‐modelling processes, including antiviral activities, but the function of the corresponding bacterial homologues was so far poorly understood. Here, we report on the protective function of a bacterial DLP , DynA from B . subtilis . We provide evidence that DynA plays an important role in a membrane surveillance system that counteracts membrane pore formation provoked by antibiotics and phages. In unstressed cells, DynA is a highly dynamic membrane‐associated protein. Upon membrane damage, DynA localizes into large and static assemblies, where DynA acts locally to counteract stress‐induced pores, presumably by inducing lipid bilayer fusion and sealing membrane gaps. Thus, lack of DynA increases the sensitivity to antibiotic exposure and phage infection. Taken together, our work suggests that DynA , and potentially other bacterial DLPs , contribute to the innate immunity of bacteria against membrane stress.