6533b86efe1ef96bd12cc9b2
RESEARCH PRODUCT
Molecular organization of selected prokaryotic S-layer proteins.
Christine EvrardHarald ClausBernhard SchlottErol AkçaJean-paul DeclercqJ. Robin HarrisTony DebaerdemaekerHelmut Königsubject
GlycanArchaeal ProteinsImmunologyMolecular Sequence DataApplied Microbiology and BiotechnologyMicrobiologyCell wallBacterial ProteinsCell WallGeneticsExtracellularMolecular BiologyGeneMembrane GlycoproteinsbiologyBacteriaBase SequenceGeneral Medicinebiology.organism_classificationArchaeaBiochemistryCytoplasmbiology.proteinProtein stabilizationBacteriaArchaeadescription
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-)protein species with molecular masses ranging from about 40 to 200 kDa that form lattices of oblique, tetragonal, or hexagonal architecture. The primary sequen ces 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 membrane. 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.Key words: prokaryotes, cell walls, S-layer (glyco-) proteins, protein stabilization.
year | journal | country | edition | language |
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2005-09-01 | Canadian journal of microbiology |