title: Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.
abstract: The pole-to-pole oscillation of the Min proteins in Escherichia coli results in the inhibition of aberrant polar division, thus facilitating placement of the division septum at the midcell. MinE of the Min system forms a ring-like structure that plays a critical role in triggering the oscillation cycle. However, the mechanism underlying the formation of the MinE ring remains unclear. This study demonstrates that MinE self-assembles into fibrillar structures on the supported lipid bilayer. The MinD-interacting domain of MinE shows amyloidogenic properties, providing a possible mechanism for self-assembly of MinE. Supporting the idea, mutations in residues Ile-24 and Ile-25 of the MinD-interacting domain affect fibril formation, membrane binding ability of MinE and MinD, and subcellular localization of three Min proteins. Additional mutations in residues Ile-72 and Ile-74 suggest a role of the C-terminal domain of MinE in regulating the folding propensity of the MinD-interacting domain for different molecular interactions. The study suggests a self-assembly mechanism that may underlie the ring-like structure formed by MinE-GFP observed in vivo.
authors.affiliation: From the Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
authors.forename: Min
authors.initials: M
authors.lastname: Zheng
authors.affiliation: Department of Material Science and Engineering, National Tsing Hua University, 101, Sec. 2, Kuang-Fu Road, Hsinchu 013, Taiwan.
authors.forename: Ya-Ling
authors.initials: YL
authors.lastname: Chiang
authors.affiliation: From the Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
authors.forename: Hsiao-Lin
authors.initials: HL
authors.lastname: Lee
authors.affiliation: From the Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.
authors.forename: Lih-Ren
authors.initials: LR
authors.lastname: Kong
authors.affiliation: From the Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan, Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan.
authors.forename: Shang-Te Danny
authors.initials: ST
authors.lastname: Hsu
authors.affiliation: Department of Material Science and Engineering, National Tsing Hua University, 101, Sec. 2, Kuang-Fu Road, Hsinchu 013, Taiwan, Institute of Physics, Academia Sinica, 128, Sec. 2, Academia Road, Taipei 115, Taiwan, and.
authors.forename: Ing-Shouh
authors.initials: IS
authors.lastname: Hwang
authors.affiliation: Department of Structural, Microbial, and Molecular Biology, University of Connecticut Health Center, Farmington, Connecticut 06032.
authors.forename: Lawrence I
authors.initials: LI
authors.lastname: Rothfield
authors.affiliation: From the Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan, Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan, ylshih10@gate.sinica.edu.tw.
authors.forename: Yu-Ling
authors.initials: YL
authors.lastname: Shih
mesh_terms: D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D008051:Lipid Bilayers; D008969:Molecular Sequence Data; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014461:Ultracentrifugation
chemical_list: D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; D008051:Lipid Bilayers; C093548:MinE protein, E coli
keywords: Bacteria; Membrane Protein; Membrane Reconstitution; Molecular Cell Biology; Protein Self-assembly