Article

The archaeal cell envelope

Molecular Biology of Archaea, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Strasse 10, D-35043 Marburg, Germany.
Nature Reviews Microbiology (Impact Factor: 23.57). 06/2011; 9(6):414-26. DOI: 10.1038/nrmicro2576
Source: PubMed

ABSTRACT

At first glance, archaea and bacteria look alike; however, the composition of the archaeal cell envelope is fundamentally different from the bacterial cell envelope. With just one exception, all archaea characterized to date have only a single membrane and most are covered by a paracrystalline protein layer. This Review discusses our current knowledge of the composition of the archaeal cell surface. We describe the wide range of cell wall polymers, O- and N-glycosylated extracellular proteins and other cell surface structures that archaea use to interact with their environment.

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Available from: Sonja-Verena Albers, Nov 11, 2014
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    • "Pseudomurein is one of the many different cell wall polymers present in Archaea, being found only in Methanobacteriales and the genus Methanopyrus [1] [2] [3] [4]. Pseudomurein has a similar overall 3-dimensional structure to murein, the predominant component of bacterial cell walls. "
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    ABSTRACT: Pseudomurein endoisopeptidases cause lysis of the cell walls of methanogens by cleaving the isopeptide bond Ala-ε-Lys in the peptide chain of pseudomurein. PeiW and PeiP are two thermostable pseudomurein endoisopeptidases encoded by phage ΨM100 of Methanothermobacter wolfei and phages ΨM1 and ΨM2 of Methanothermobacter marburgensis, respectively. A continuous assay using synthetic peptide substrates was developed and used in the biochemical characterisation of recombinant PeiW and PeiP. The advantages of these synthetic peptide substrates over natural substrates are sensitivity, high purity, and characterisation and the fact that they are more easily obtained than natural substrates. In the presence of a reducing agent, purified PeiW and PeiP each showed similar activity under aerobic and anaerobic conditions. Both enzymes required a divalent metal for activity and showed greater thermostability in the presence of Ca2+. PeiW and PeiP involve a cysteine residue in catalysis and have a monomeric native conformation. The kinetic parameters, K M and k cat, were determined, and the ε-isopeptide bond between alanine and lysine was confirmed as the bond lysed by these enzymes in pseudomurein. The new assay may have wider applications for the general study of peptidases and the identification of specific methanogens susceptible to lysis by specific pseudomurein endoisopeptidases.
    Full-text · Article · Sep 2015 · Archaea (Vancouver, B.C.)
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    • "In almost all archaea, the cell is covered by a proteinous surface layer (S-layer) which maintains the cell shape and interacts with the environment (Albers and Meyer 2011; Klingl 2014). Apart from a few species, archaeal S-layers are composed of a single membrane associated protein or glycoprotein species, called S-layer protein or glycoprotein (Albers and Meyer 2011). The archaeal S-layer glycoprotein has been widely studied (Jarrell et al. 2010; Kandiba and Eichler 2014). "

    Full-text · Dataset · Sep 2015
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    • "In almost all archaea, the cell is covered by a proteinous surface layer (S-layer) which maintains the cell shape and interacts with the environment (Albers and Meyer 2011; Klingl 2014). Apart from a few species, archaeal S-layers are composed of a single membrane associated protein or glycoprotein species, called S-layer protein or glycoprotein (Albers and Meyer 2011). The archaeal S-layer glycoprotein has been widely studied (Jarrell et al. 2010; Kandiba and Eichler 2014). "

    Full-text · Dataset · Sep 2015
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