Self-propelling bacteria are a nanotechnology dream. These unicellular organisms are not just capable of living and reproducing, but they can swim very efficiently, sense the environment, and look for food, all packaged in a body measuring a few microns. Before such perfect machines can be artificially assembled, researchers are beginning to explore new ways to harness bacteria as propelling units for microdevices. Proposed strategies require the careful task of aligning and binding bacterial cells on synthetic surfaces in order to have them work cooperatively. Here we show that asymmetric environments can produce a spontaneous and unidirectional rotation of nanofabricated objects immersed in an active bacterial bath. The propulsion mechanism is provided by the self-assembly of motile Escherichia coli cells along the rotor boundaries. Our results highlight the technological implications of active matter's ability to overcome the restrictions imposed by the second law of thermodynamics on equilibrium passive fluids.
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http://dx.doi.org/10.1073/pnas.0910426107 | DOI Listing |
Cell Host Microbe
December 2024
National Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, 430070 Wuhan, China. Electronic address:
The sensing of pathogens is the first step for any immune response. A recent paper in Cell reveals that the bacterial Hachiman anti-phage defense system deploys a helicase subunit to sense phage invasion via 3' DNA recognition and subsequent domain rotation to enable nuclease activation.
View Article and Find Full Text PDFJ Mol Biol
April 2024
Department of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, 650 W. Baltimore Street, Baltimore, MD 21201, USA. Electronic address:
Dedicated translocase channels are nanomachines that often, but not always, unfold and translocate proteins through narrow pores across the membrane. Generally, these molecular machines utilize external sources of free energy to drive these reactions, since folded proteins are thermodynamically stable, and once unfolded they contain immense diffusive configurational entropy. To catalyze unfolding and translocate the unfolded state at appreciable timescales, translocase channels often utilize analogous peptide-clamp active sites.
View Article and Find Full Text PDFBiochem Soc Trans
October 2023
Department of Physics and Astronomy, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, South Korea.
Structural maintenance of chromosome (SMC) proteins play a key roles in the chromosome organization by condensing two meters of DNA into cell-sized structures considered as the SMC protein extrudes DNA loop. Recent sequencing-based high-throughput chromosome conformation capture technique (Hi-C) and single-molecule experiments have provided direct evidence of DNA-loop extrusion. However, the molecular mechanism by which SMCs extrude a DNA loop is still under debate.
View Article and Find Full Text PDFFront Mol Biosci
August 2023
Departamento de Biología, Facultad de Química, Ciudad Universitaria, Universidad Nacional Autónoma de México (U.N.A.M.), Ciudad de México, México.
The subunit is a potent inhibitor of the FF-ATPase of (PdFF-ATPase) and related -proteobacteria different from the other two canonical inhibitors of bacterial () and mitochondrial (IF) FF-ATPases. mimics mitochondrial IF in its inhibitory N-terminus, blocking the PdFF-ATPase activity as a unidirectional pawl-ratchet and allowing the PdFF-ATP synthase turnover. is essential for the respiratory growth of , as we showed by a knockout.
View Article and Find Full Text PDFCommun Biol
August 2023
Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often polymerized by the inner membrane bound Wzy-dependent pathway. By employing cryo-electron microscopy we show that WzzE, the co-polymerase component of this pathway that is responsible for the length modulation of the enterobacterial common antigen, is octameric with alternating up-down conformations of its L4 loops. The alternating up-down nature of these essential loops, located at the top of the periplasmic bell, are modulated by clashing helical faces between adjacent protomers that flank the L4 loops around the octameric periplasmic bell.
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