title: MscS-like proteins control plastid size and shape in Arabidopsis thaliana.
abstract: BACKGROUND
  Mechanosensitive (MS) ion channels provide a mechanism for the perception of mechanical stimuli such as sound, touch, and osmotic pressure. The bacterial MS ion channel MscS opens in response to increased membrane tension and serves to protect against cellular lysis during osmotic downshock. MscS-like proteins are found widely in bacterial and archaeal species and have also been identified in fission yeast and plants. None of the eukaryotic members of the family have yet been characterized.
  
  
  RESULTS
  Here, we characterize two MscS-like (MSL) proteins from Arabidopsis thaliana, MSL2 and MSL3. MSL3 can rescue the osmotic-shock sensitivity of a bacterial mutant lacking MS-ion-channel activity, suggesting that it functions as a mechanosensitive ion channel. Arabidopsis plants harboring insertional mutations in both MSL3 and MSL2 show abnormalities in the size and shape of plastids, which are plant-specific endosymbiotic organelles responsible for photosynthesis, gravity perception, and numerous metabolic reactions. MSL2-GFP and MSL3-GFP are localized to discrete foci on the plastid envelope and colocalize with the plastid division protein AtMinE.
  
  
  CONCLUSIONS
  Our data support a model wherein MSL2 and MSL3 control plastid size, shape, and perhaps division during normal plant development by altering ion flux in response to changes in membrane tension. We propose that MscS family members have evolved new roles in plants since the endosymbiotic event that gave rise to plastids.
authors.affiliation: Division of Biology, 156-29, California Institute of Technology, 1200 E. California Blvd., Pasadena, California 91125, USA.
authors.forename: Elizabeth S
authors.initials: ES
authors.lastname: Haswell
authors.forename: Elliot M
authors.initials: EM
authors.lastname: Meyerowitz
mesh_terms: D017360:Arabidopsis / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure*; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D001483:Base Sequence; D018797:Cell Cycle Proteins / Q000378:metabolism; D048430:Cell Shape; D048429:Cell Size; D002736:Chloroplasts / Q000378:metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry; D005838:Genotype; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D040542:Mechanotransduction, Cellular; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D009997:Osmotic Pressure; D010802:Phylogeny; D030821:Plants, Genetically Modified / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure; D018087:Plastids / Q000737:chemistry / Q000648:ultrastructure*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D016415:Sequence Alignment; D017385:Sequence Homology
chemical_list: D029681:Arabidopsis Proteins; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; D007473:Ion Channels; C508380:MSL2 protein, Arabidopsis; C508381:MSL3 protein, Arabidopsis; C465003:MinE1 protein, Arabidopsis; C469542:MscS protein, E coli; D011993:Recombinant Fusion Proteins