The actin homologue MreB organizes the bacterial cell membrane

被引:170
作者
Strahl, Henrik [1 ]
Buermann, Frank [2 ]
Hamoen, Leendert W. [1 ,3 ]
机构
[1] Univ Newcastle, Inst Cell & Mol Biosci, Ctr Bacterial Cell Biol, Newcastle Upon Tyne NE2 4AX, Tyne & Wear, England
[2] Max Planck Inst Biochem, D-82152 Martinsried, Germany
[3] Univ Amsterdam, Swammerdam Inst Life Sci, NL-1098 XH Amsterdam, Netherlands
来源
NATURE COMMUNICATIONS | 2014年 / 5卷
基金
英国惠康基金; 英国生物技术与生命科学研究理事会;
关键词
BACILLUS-SUBTILIS CELLS; PROTON PERMEABILITY; LIPID DOMAINS; NILE RED; PROTEINS; WALL; LOCALIZATION; PROBE; PHOSPHATIDYLGLYCEROL; HOMEOSTASIS;
D O I
10.1038/ncomms4442
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The eukaryotic cortical actin cytoskeleton creates specific lipid domains, including lipid rafts, which determine the distribution of many membrane proteins. Here we show that the bacterial actin homologue MreB displays a comparable activity. MreB forms membrane-associated filaments that coordinate bacterial cell wall synthesis. We noticed that the MreB cytoskeleton influences fluorescent staining of the cytoplasmic membrane. Detailed analyses combining an array of mutants, using specific lipid staining techniques and spectroscopic methods, revealed that MreB filaments create specific membrane regions with increased fluidity (RIFs). Interference with these fluid lipid domains (RIFs) perturbs overall lipid homeostasis and affects membrane protein localization. The influence of MreB on membrane organization and fluidity may explain why the active movement of MreB stimulates membrane protein diffusion. These novel MreB activities add additional complexity to bacterial cell membrane organization and have implications for many membrane-associated processes.
引用
收藏
页数:11
相关论文
共 69 条
  • [41] Sculpting the Bacterial Cell
    Margolin, William
    [J]. CURRENT BIOLOGY, 2009, 19 (17) : R812 - R822
  • [42] Lipid domains in bacterial membranes
    Matsumoto, Kouji
    Kusaka, Jin
    Nishibori, Ayako
    Hara, Hiroshi
    [J]. MOLECULAR MICROBIOLOGY, 2006, 61 (05) : 1110 - 1117
  • [43] Domain formation induced by the adsorption of charged proteins on mixed lipid membranes
    Mbamala, EC
    Ben-Shaul, A
    May, S
    [J]. BIOPHYSICAL JOURNAL, 2005, 88 (03) : 1702 - 1714
  • [44] Membrane curvature and mechanisms of dynamic cell membrane remodelling
    McMahon, HT
    Gallop, JL
    [J]. NATURE, 2005, 438 (7068) : 590 - 596
  • [45] Crucial Role for Membrane Fluidity in Proliferation of Primitive Cells
    Mercier, Romain
    Dominguez-Cuevas, Patricia
    Errington, Jeff
    [J]. CELL REPORTS, 2012, 1 (05): : 417 - 423
  • [46] Cardiolipin membrane domains in prokaryotes and eukaryotes
    Mileykovskaya, Eugenia
    Dowhan, William
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2009, 1788 (10): : 2084 - 2091
  • [47] The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli
    Mohammadi, Tamimount
    Karczmarek, Aneta
    Crouvoisier, Muriel
    Bouhss, Ahmed
    Mengin-Lecreulx, Dominique
    Den Blaauwen, Tanneke
    [J]. MOLECULAR MICROBIOLOGY, 2007, 65 (04) : 1106 - 1121
  • [48] Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
    Muchova, Katarina
    Wilkinson, Anthony J.
    Barak, Imrich
    [J]. FEMS MICROBIOLOGY LETTERS, 2011, 325 (01) : 92 - 98
  • [49] Membrane localization and dynamics of Nile Red: Effect of cholesterol
    Mukherjee, Soumi
    Raghuraman, H.
    Chattopadhyay, Amitabha
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2007, 1768 (01): : 59 - 66
  • [50] PHASE FLUCTUATION IN PHOSPHOLIPID-MEMBRANES REVEALED BY LAURDAN FLUORESCENCE
    PARASASSI, T
    DE STASIO, G
    DUBALDO, A
    GRATTON, E
    [J]. BIOPHYSICAL JOURNAL, 1990, 57 (06) : 1179 - 1186