SignificanceSingle-celled microorganisms are important in ecosystems, and their behaviors impact the Earth’s environments. To survive in harsh environments, these organisms frequently act as though exercising discretion. How do they achieve such intelligent behaviors? In this work, we focused on the accumulation of ciliates on solid/fluid interfaces, where they can obtain sufficient nutrients and a stable environment. This phenomenon is not described in the standard hydrodynamics of microswimmers. Our experiment and simulation revealed that simple principles, the anisotropic shape of the cell and the mechanosensing nature of cilia, induce the accumulation of ciliates on solid/fluid interfaces. The contribution of our work is that a simple response of the cellular apparatus and fluid dynamics explain the apparently clever behavior of ciliates.
Amoeboid locomotion is one of the typical modes of biological cell migration. Cytoplasmic sol–gel conversion of an actomyosin system is thought to play an important role in locomotion. However, the mechanisms underlying sol–gel conversion, including trigger, signal, and regulating factors, remain unclear. We developed a novel model system in which an actomyosin fraction moves like an amoeba in a cytoplasmic extract. Rheological study of this model system revealed that the actomyosin fraction exhibits shear banding: the sol–gel state of actomyosin can be regulated by shear rate or mechanical force. Furthermore, study of the living cell indicated that the shear-banding property also causes sol–gel conversion with the same order of magnitude as that of shear rate. Our results suggest that the inherent sol–gel transition property plays an essential role in the self-regulation of autonomous translational motion in amoeba.
Some types of ciliates accumulate on solid/fluid interfaces. This behavior is advantageous to survival in nature due to the presence of sufficient nutrition and stable environments. Recently, the accumulating mechanisms of Tetrahymena pyriformis at the interface were investigated. The synergy of the ellipsoidal shape of the cell body and the mechanosensing feature of the cilia allow for cells to slide on interfaces, and the sliding behavior leads to cell accumulation on the interfaces. Here, to examine the generality of the sliding behavior of ciliates, we characterized the behavior of Paramecium caudatum, which is a commonly studied ciliate. Our experimental and numerical results confirmed that P. caudatum also slid on the solid/fluid interface by using the same mechanism as T. pyriformis. In addition, we evaluated the effects of cellular ellipticity on their behaviors near the wall with a phase diagram produced via numerical simulation.
BackgroundAn ancestral trait of eukaryotic cells is the presence of mitochondria as an essential element for function and survival. Proper functioning of mitochondria depends on the import of nearly all proteins that is performed by complexes located in both mitochondrial membranes. The complexes have been proposed to contain subunits formed by proteins common to all eukaryotes and additional subunits regarded as lineage specific. Since Amoebozoa is poorly sampled for the complexes we investigated the outer membrane complexes, namely TOM, TOB/SAM and ERMES complexes, using available genome and transcriptome sequences, including transcriptomes assembled by us.ResultsThe results indicate differences in the organization of the Amoebozoa TOM, TOB/SAM and ERMES complexes, with the TOM complex appearing to be the most diverse. This is reflected by differences in the number of involved subunits and in similarities to the cognate proteins of representatives from different supergroups of eukaryotes.ConclusionsThe obtained results clearly demonstrate structural variability/diversity of these complexes in the Amoebozoa lineage and the reduction of their complexity as compared with the same complexes of model organisms.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-2402-2) contains supplementary material, which is available to authorized users.
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