Reference : Molecular organization of selected prokaryotic S-Iayer proteins
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Molecular organization of selected prokaryotic S-Iayer proteins
Claus, Harald [Johannes Gutenberg Universität, Mainz > > > >]
Akça, Erol [Johannes Gutenberg Universität, Mainz > > > >]
Debaerdemaeker, Tony [Universität Ulm > > > >]
Evrard, Christine mailto [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale > >]
Declercq, Jean-Paul mailto [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale > >]
Harris, J. Robin [Johannes Gutenberg Universität, Mainz > > > >]
Schlott, Bernhard [Institut für Molekulare Biotechnologie, Jena > > > >]
König, Helmut [Johannes Gutenberg Universität, Mainz > > > >]
Canadian Journal of Microbiology
NRC Research Press
Yes (verified by ORBi)
[en] prokaryotes ; cell walls ; S-layer (glyco-) proteins ; protein stabilization
[en] Regular crystalline surface layers (S-layers) are widespread among prokaryotes and probably represent the earliest cell wall structures. S-layer genes have been found in approximately 400 different species of the prokaryotic domains bacteria and archaea. S-layers usually consist of a single (glyco-rprotein species with molecular masses ranging from about 40 to 200 kDa that form lattices of oblique, tetragonal, or hexagonal architecture. The primary sequences of hyperthermophilic archaeal species exhibit some characteristic signatures, Further adaptations to their specific environments occur by various post-translational modifications, such as linkage of glycans, lipids, phosphate, and sulfate groups to the protein or by proteolytic processing. Specific domains direct the anchoring of the S-layer to the underlying cell wall components and transport across the cytoplasma memhrane. In addition to their presumptive original role as protective coats in archaea and bacteria, they have adapted new functions, e.g., as molecular sieves, attachment sites for extracellular enzymes, and virulence factors.

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