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FlhE functions as a chaperone to prevent formation of periplasmic flagella in Gram-negative bacteria.
Halte, Manuel; Andrianova, Ekaterina P; Goosmann, Christian; Chevance, Fabienne F V; Hughes, Kelly T; Zhulin, Igor B; Erhardt, Marc.
Affiliation
  • Halte M; Institute of Biology, Humboldt-Universität zu Berlin, Philippstr. 13, 10115, Berlin, Germany. manuel.halte@hu-berlin.de.
  • Andrianova EP; Department of Microbiology, The Ohio State University, Columbus, OH, 43210, USA.
  • Goosmann C; Max Planck Institute for Infection Biology, Charitéplatz 1, 10117, Berlin, Germany.
  • Chevance FFV; School of Biological Sciences, University of Utah, Salt Lake City, UT, USA.
  • Hughes KT; School of Biological Sciences, University of Utah, Salt Lake City, UT, USA.
  • Zhulin IB; Department of Microbiology, The Ohio State University, Columbus, OH, 43210, USA.
  • Erhardt M; Institute of Biology, Humboldt-Universität zu Berlin, Philippstr. 13, 10115, Berlin, Germany. marc.erhardt@hu-berlin.de.
Nat Commun ; 15(1): 5921, 2024 Jul 14.
Article in En | MEDLINE | ID: mdl-39004688
ABSTRACT
The bacterial flagellum, which facilitates motility, is composed of ~20 structural proteins organized into a long extracellular filament connected to a cytoplasmic rotor-stator complex via a periplasmic rod. Flagellum assembly is regulated by multiple checkpoints that ensure an ordered gene expression pattern coupled to the assembly of the various building blocks. Here, we use epifluorescence, super-resolution, and transmission electron microscopy to show that the absence of a periplasmic protein (FlhE) prevents proper flagellar morphogenesis and results in the formation of periplasmic flagella in Salmonella enterica. The periplasmic flagella disrupt cell wall synthesis, leading to a loss of normal cell morphology resulting in cell lysis. We propose that FlhE functions as a periplasmic chaperone to control assembly of the periplasmic rod, thus preventing formation of periplasmic flagella.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Molecular Chaperones / Periplasm / Flagella Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2024 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Molecular Chaperones / Periplasm / Flagella Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2024 Document type: Article Affiliation country:
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