CbrA Is a Flavin Adenine Dinucleotide Protein That Modifies the Escherichia coli Outer Membrane and Confers Specific Resistance to Colicin M

Autor: Stephanie Helbig, Volkmar Braun, Moritz Ammelburg, Klaus Hantke
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Popis: Colicin M (Cma) is a protein toxin produced byEscherichia colithat kills sensitiveE. colicells by inhibiting murein biosynthesis in the periplasm. Recombinant plasmids carryingcbrA(formerlyyidS) strongly increased resistance of cells to Cma, whereas deletion ofcbrAincreased Cma sensitivity. Transcription ofcbrAis positively controlled by the two-component CreBC system. A ΔcreBmutant was highly Cma sensitive because little CbrA was synthesized. Treatment of CbrA-overproducing cells by osmotic shock failed to render cells Cma sensitive because the cells were resistant to osmotic shock. In a natural environment with a growth-limiting nutrient supply, cells producing CbrA defend themselves against colicin M synthesized by competing cells. Isolated CbrA is a protein with noncovalently bound flavin adenine dinucleotide. Sequence comparison and structure prediction assign the closest relative of CbrA with a known crystal structure as digeranylgeranyl-glycerophospholipid reductase ofThermoplasma acidophilum. CbrA is found inEscherichia coli,Citrobacter, andSalmonella bongoribut not in other enterobacteria. The next homologs with the highest identity (over 50%) are found in the anaerobicClostridium botulinumgroup 1 and a few otherFirmicutes.
Databáze: OpenAIRE