title: A Diguanylate Cyclase Acts as a Cell Division Inhibitor in a Two-Step Response to Reductive and Envelope Stresses.
abstract: Cell division arrest is a universal checkpoint in response to environmental assaults that generate cellular stress. In bacteria, the cyclic di-GMP (c-di-GMP) signaling network is one of several signal transduction systems that regulate key processes in response to extra-/intracellular stimuli. Here, we find that the diguanylate cyclase YfiN acts as a bifunctional protein that produces c-di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli YfiN localizes to the Z ring by interacting with early division proteins and stalls cell division by preventing the initiation of septal peptidoglycan synthesis. These studies reveal a new role for a diguanylate cyclase in responding to environmental change, as well as a novel mechanism for arresting cell division.
  
  
  
  While the major role of c-di-GMP signaling is to control the decision to move freely or settle in a biofilm, recent studies show a broader range of output functions for c-di-GMP signaling. This work reports an unexpected second role for YfiN, a conserved diguanylate cyclase in Gram-negative bacteria, known to contribute to persistence in the host. We find that YfiN acts as a cell division inhibitor in response to envelope stress. Unlike known cell division inhibitors, the interaction of YfiN with cell division proteins retains the Z ring at the midcell but prevents septal invagination. The new function of YfiN not only emphasizes the versatility of c-di-GMP signaling but describes a novel mechanism for a cell division checkpoint.
authors: Department of Molecular Biosciences and Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, USA.
authors: Hyo Kyung
authors: HK
authors: Kim
authors: Department of Molecular Biosciences and Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, USA rasika@austin.utexas.edu.
authors: Rasika M
authors: RM
authors: Harshey
mesh_terms: D018797:Cell Cycle Proteins / Q000378:metabolism*; D002455:Cell Division; D002473:Cell Wall / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism; D019761:Phosphorus-Oxygen Lyases / Q000378:metabolism*; D013312:Stress, Physiological
chemical_list: D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; D010457:Peptidoglycan; D019761:Phosphorus-Oxygen Lyases; C060720:diguanylate cyclase