作者: Osigwe Esue , Laura Rupprecht , Sean X. Sun , Denis Wirtz
DOI: 10.1371/JOURNAL.PONE.0008855
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摘要: Background Crescentin, the recently discovered bacterial intermediate filament protein, organizes into an extended filamentous structure that spans length of bacterium Caulobacter crescentus and plays a critical role in defining its curvature. The mechanism by which crescentin mediates cell curvature whether structures are dynamic and/or polar not fully understood. Methodology/Principal Findings Using light microscopy, electron microscopy quantitative rheology, we investigated mechanics dynamics structures. Live-cell reveals forms vivo undergo slow remodeling. exchange subunits between these pool unassembled is during life cycle however; vitro assembly gelation C. rapid. Moreover, elastic, solid-like, and, like other filaments, can recover significant portion their network elasticity after shear. efficiency largely unaffected monovalent cations (K+, Na+), but enhanced divalent (Mg2+, Ca2+), suggesting kinetics micromechanics depend on valence ions present solution. Conclusions/Significance These results indicate labile, stiff, low dissociation rate from established controls remodeling crescentus.