Establishment of an axis of cell polarity and differentiation of the cell poles are fundamental aspects of cellular development in many organisms. We compared the effects of two bacterial cytoskeletal-like systems, the MreB and MinCDE systems, on these processes in Escherichia coli. We report that the Min proteins are capable of establishing an axis of oscillation that is the initial step in establishment of polarity in spherical cells, in a process that is independent of the MreB cytoskeleton. In contrast, the MreB system is required for establishment of the rod shape of the cell and for polar targeting of other polar constituents, such as the Shigella virulence factor IcsA and the aspartate chemoreceptor Tar, in a process that is independent of the Min system. Thus, the two bacterial cytoskeletal-like systems act independently on different aspects of cell polarization.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1111/j.1365-2958.2005.04841.x | DOI Listing |
Adv Mater
June 2020
MIIT Key Laboratory of Critical Materials Technology for New Energy Conversion and Storage, School of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin, 150001, China.
The ability of living organisms to perform structure, energy, and information-related processes for molecular self-assembly through compartmentalization and chemical transformation can possibly be mimicked via artificial cell models. Recent progress in the development of various types of functional microcompartmentalized ensembles that can imitate rudimentary aspects of living cells has refocused attention on the important question of how inanimate systems can transition into living matter. Hence, herein, the most recent advances in the construction of protein-bounded microcompartments (proteinosomes), which have been exploited as a versatile synthetic chassis for integrating a wide range of functional components and biochemical machineries, are critically summarized.
View Article and Find Full Text PDFMol Microbiol
November 2008
Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06032, USA.
Ribonuclease E (RNase E) is a component of the Escherichia coli RNA degradosome, a multiprotein complex that also includes RNA helicase B (RhlB), polynucleotide phosphorylase (PNPase) and enolase. The degradosome plays a key role in RNA processing and degradation. The degradosomal proteins are organized as a cytoskeletal-like structure within the cell that has been thought to be associated with the cytoplasmic membrane.
View Article and Find Full Text PDFVirology
February 2008
School of Life Sciences, Oxford Brookes University, Oxford, OX3 0BP, UK.
The role of the microtubule-associated P10 protein of baculoviruses is not yet understood. P10 has previously been linked with the formation of a number of cytoskeletal-like or cytoskeleton-associated structures in the nucleus and cytoplasm, thought to be involved in the morphogenesis of virus polyhedral occlusion bodies. The formation of these structures was studied by immunofluorescence laser scanning confocal microscopy in TN368 cells, a model system amenable to the study of virus interaction with the host cell cytoskeleton.
View Article and Find Full Text PDFPhys Rev E Stat Nonlin Soft Matter Phys
July 2007
Department of Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
We introduce a stochastic approach for self-assembly in systems far from equilibrium. The building blocks are represented by a lattice of discrete variables (Potts-like spins), and physically meaningful mechanisms are obtained by restricting transitions through spatially local rules based on experimental data. We use the method to study nucleation of filopodia-like bundles in a system consisting of purified actin, fascin, actin-related protein 2/3 , and beads coated with Wiskott-Aldrich syndrome protein.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2007
Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06032, USA.
RNaseE is the main component of the RNA degradosome of Escherichia coli, which plays an essential role in RNA processing and decay. Localization studies showed that RNaseE and the other known degradosome components (RNA helicase B, polynucleotide phosphorylase, and enolase) are organized as helical filamentous structures that coil around the length of the cell. These resemble the helical structures formed by the MreB and MinD cytoskeletal proteins.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!