Exclusion of assembled MreB by anionic phospholipids at cell poles confers cell polarity for bidirectional growth.
Cell polarity determines the direction of cell growth in bacteria. MreB actin spatially regulates peptidoglycan synthesis to enable cells to elongate bidirectionally. MreB densely localizes in the cylindrical part of the rod cell and not in polar regions in Escherichia coli. When treated with A22, which inhibits MreB polymerization, rod-shaped cells became round and MreB was diffusely distributed throughout the cytoplasmic membrane. A22 removal resulted in restoration of the rod shape. Initially, diffuse MreB started to re-assemble, and MreB-free zones were subsequently observed in the cytoplasmic membrane. These MreB-free zones finally became cell poles, allowing the cells to elongate bidirectionally. When MreB was artificially located at the cell poles, an additional pole was created, indicating that artificial localization of MreB at the cell pole induced local peptidoglycan synthesis. It was found that the anionic phospholipids (aPLs), phosphatidylglycerol and cardiolipin, which were enriched in cell poles preferentially interact with monomeric MreB compared with assembled MreB in vitro. MreB tended to localize to cell poles in cells lacking both aPLs, resulting in production of Y-shaped cells. Their findings indicated that aPLs exclude assembled MreB from cell poles to establish cell polarity, thereby allowing cells to elongate in a particular direction.
Department of Life Science, College of Science, Rikkyo University, 3-34-1 Nishi-Ikebukuro, Toshima-ku, Tokyo, 171-8501, Japan.
Takuma
T
Kawazura
Department of Life Science, College of Science, Rikkyo University, 3-34-1 Nishi-Ikebukuro, Toshima-ku, Tokyo, 171-8501, Japan.
Kanon
K
Matsumoto
Department of Life Science, College of Science, Rikkyo University, 3-34-1 Nishi-Ikebukuro, Toshima-ku, Tokyo, 171-8501, Japan.
Koki
K
Kojima
Department of Life Science, College of Science, Rikkyo University, 3-34-1 Nishi-Ikebukuro, Toshima-ku, Tokyo, 171-8501, Japan.
Fumiya
F
Kato
Department of Life Science, College of Science, Rikkyo University, 3-34-1 Nishi-Ikebukuro, Toshima-ku, Tokyo, 171-8501, Japan.
Tomomi
T
Kanai
Microbial Genetics Laboratory, Genetic Strains Research Center, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka, 411-8540, Japan.|Department of Genetics, The Graduate University for Advanced Studies, Sokendai, 1111 Yata, Mishima, Shizuoka, 411-8540, Japan.
Hironori
H
Niki
Department of Life Science, College of Science, Rikkyo University, 3-34-1 Nishi-Ikebukuro, Toshima-ku, Tokyo, 171-8501, Japan.
Daisuke
http://orcid.org/0000-0002-8558-7175
D
Shiomi
D002462:Cell Membrane / Q000378:metabolism; D016764:Cell Polarity / Q000502:physiology*; D048430:Cell Shape / Q000502:physiology; D002473:Cell Wall / Q000378:metabolism; D004926:Escherichia coli / Q000166:cytology* / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D058105:Polymerization; D013890:Thiourea / Q000031:analogs & derivatives / Q000494:pharmacology
D029968:Escherichia coli Proteins; D010743:Phospholipids; C078473:MreB protein, E coli; C015799:2,6-dichlorobenzylthiopseudourea; D013890:Thiourea