Literature DB >> 16983198

Cytoskeletal elements in bacteria Mycoplasma pneumoniae, Thermoanaerobacterium sp., and Escherichia coli as revealed by electron microscopy.

Frank Mayer1.   

Abstract

Recently, electron microscopic studies on the eubacteria Mycoplasma pneumoniae, Thermoanaerobacterium sp., and Escherichia coli have revealed the existence of cytoskeletal elements so far unknown in prokaryotes. The wall-less bacterium M. pneumoniae contains, in close vicinity to the inner face of the cytoplasmic membrane, a helically organized lining composed of protein elements that form a regular network of meshes that encloses the entire cytoplasm. Numerous regularly spaced pin-like structural elements, the stalks with terminal knobs, connect the lining with the cytoplasmic membrane. In this bacterium, a specific rod-like structural element is located in the tip region. Occasionally, it is bent or twisted. It consists of two matching blade-like sub-elements. A number of parallel linkers, extending from the edges of the rod, make contact with the lining. The proximal end of the rod is attached to a wheel-like complex. Fibrils originating from the wheel cross the cytoplasm and make contact with the lining. E. coli contains a similar helically organized lining close to the inner face of the cytoplasmic membrane. Groups of ribosomes (polysomes) were seen to be attached to the helical elements of the lining. A feature that is common to both bacteria and to Thermoanaerobacterium sp. appears to be that the lining and the fibrils crossing the cytoplasm contain a high number of copies of the bacterial elongation factor Tu (EF-Tu). This indicates that this protein may play an important role as a structural element in bacterial cytoskeletons. This notion was supported by experiments in which the cytoskeleton in E. coli was destabilized by induced expression of truncated EF-Tu, with the consequence of cell lysis, and by the finding that in vitro polymerization of monomeric EF-Tu into protofilaments was hindered in a mixture of full-size EF-Tu and truncated EF-Tu consisting of domain 3 only. Current research and developmental efforts are aimed at the design of a new class of antibacterial drugs, acting by destabilization of the EF-Tu-containing bacterial cytoskeleton, and of an innovative mode of inducible lysis of recombinant bacteria by controlled destabilization of the EF-Tu-containing cytoskeleton.

Entities:  

Mesh:

Substances:

Year:  2006        PMID: 16983198     DOI: 10.1159/000094057

Source DB:  PubMed          Journal:  J Mol Microbiol Biotechnol        ISSN: 1464-1801


  9 in total

1.  New approaches to the problem of generating coherent, reproducible phenotypes.

Authors:  Vic Norris; Ghislain Gangwe Nana; Jean-Nicolas Audinot
Journal:  Theory Biosci       Date:  2013-06-21       Impact factor: 1.919

2.  Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein.

Authors:  Hervé Joël Defeu Soufo; Christian Reimold; Uwe Linne; Tobias Knust; Johannes Gescher; Peter L Graumann
Journal:  Proc Natl Acad Sci U S A       Date:  2010-01-28       Impact factor: 11.205

3.  Molecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cells.

Authors:  Vic Norris; Rosetta N Reusch; Kazuei Igarashi; Robert Root-Bernstein
Journal:  Biol Direct       Date:  2014-12-04       Impact factor: 4.540

4.  Chromosome Replication in Escherichia coli: Life on the Scales.

Authors:  Vic Norris; Patrick Amar
Journal:  Life (Basel)       Date:  2012-10-29

5.  Epitope Mapping of Streptococcus agalactiae Elongation Factor Tu Protein Recognized by Human Sera.

Authors:  Marcelina Pyclik; Sabina Górska; Ewa Brzozowska; Anna Dobrut; Jarosław Ciekot; Andrzej Gamian; Monika Brzychczy-Włoch
Journal:  Front Microbiol       Date:  2018-02-06       Impact factor: 5.640

6.  Generation of Bacterial Diversity by Segregation of DNA Strands.

Authors:  Vic Norris; Camille Ripoll
Journal:  Front Microbiol       Date:  2021-03-22       Impact factor: 5.640

7.  A structural framework for a near-minimal form of life: mass and compositional analysis of the helical mollicute Spiroplasma melliferum BC3.

Authors:  Shlomo Trachtenberg; Peter Schuck; Terry M Phillips; S Brian Andrews; Richard D Leapman
Journal:  PLoS One       Date:  2014-02-21       Impact factor: 3.240

8.  Integrated Information and Prospects for Gliding Mechanism of the Pathogenic Bacterium Mycoplasma pneumoniae.

Authors:  Makoto Miyata; Tasuku Hamaguchi
Journal:  Front Microbiol       Date:  2016-06-28       Impact factor: 5.640

Review 9.  Immunogenic Proteins of Group B Streptococcus-Potential Antigens in Immunodiagnostic Assay for GBS Detection.

Authors:  Anna Dobrut; Monika Brzychczy-Włoch
Journal:  Pathogens       Date:  2021-12-31
  9 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.