S layer studies on three species of <i>Methanococcus</i> living at different temperatures

Nußer, Elisabeth; König, Helmut

doi:10.1139/m87-043

Cited by 28 publications

(5 citation statements)

References 22 publications

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“…A number of studies have compared the S-layer of mesophilic and thermophilic methanogens. The S-layer of Methanococcus vannielii, Methanococcus thermolithotrophicus , and Methanocaldococcus jannaschii have shown comparable chemical and amino acid composition ( Nußer and König, 1987 ; Akca et al, 2002 ), despite having different optimal growth temperatures (37, 65, and 85°C, respectively). There is no indication that these S-layer proteins are glycosylated when using PAS staining for detection ( Akca et al, 2002 ).…”

Section: Euryarchaeotamentioning

confidence: 99%

Archaeal S-Layers: Overview and Current State of the Art

et al. 2017

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In contrast to bacteria, all archaea possess cell walls lacking peptidoglycan and a number of different cell envelope components have also been described. A paracrystalline protein surface layer, commonly referred to as S-layer, is present in nearly all archaea described to date. S-layers are composed of only one or two proteins and form different lattice structures. In this review, we summarize current understanding of archaeal S-layer proteins, discussing topics such as structure, lattice type distribution among archaeal phyla and glycosylation. The hexagonal lattice type is dominant within the phylum Euryarchaeota, while in the Crenarchaeota this feature is mainly associated with specific orders. S-layers exclusive to the Crenarchaeota have also been described, which are composed of two proteins. Information regarding S-layers in the remaining archaeal phyla is limited, mainly due to organism description through only culture-independent methods. Despite the numerous applied studies using bacterial S-layers, few reports have employed archaea as a study model. As such, archaeal S-layers represent an area for exploration in both basic and applied research.

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Section: Euryarchaeotamentioning

confidence: 99%

Archaeal S-Layers: Overview and Current State of the Art

et al. 2017

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“…The S-layer protein had an apparent molecular mass of 74 kDa, which is similar to that previously assigned to the M. voltae S-layer protein (7). In a Western blot (immunoblot), the protein reacted with a purified antibody preparation that we had used in our gene cloning (3).…”

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confidence: 53%

Identification of the Methanococcus voltae S-layer structural gene

et al. 1994

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We have established that the gene which we had previously identified as encoding the Methanococcus voltae P-type ATPase is, in fact, the structural gene for the M. voitae S-layer protein. This conclusion is based on a comparison of the N-terminal sequence of S-layer protein prepared by two independent methods with that derived from the nucleotide sequence of the cloned gene. This conclusion was further supported by immunocytochemical localization of the antigen directed against the antibodies used in the cloning experiments.High-resolution electron microscopy of thin-sectioned, freeze-etched, freeze-dried, and shadowed or negatively stained prokaryotes has shown that the outermost cell envelope in many species of bacteria and archaea consists of a crystalline cell surface layer, designated the S-layer. In most archaea the S-layer is the only cell envelope component outside the cytoplasmic membrane (1, 12). Among members of the methanogenic archaean order Methanococcales, the S-layer is composed of a regular hexagonal array of protein subunits that completely covers the cell surface (4, 5). Among the methanogens, primary sequence information is available only for the related species Methanothermus fervidus and Methanothermus sociabilis (2).Structural analysis. We have reported the nucleotide sequence of a gene that we believed was the structural gene for a membrane-associated Methanococcus voltae P-type ATPase (GenBank accession number M59200) (3). We now believe that the gene that we cloned encodes the M. voltae S-layer protein.Patel and coworkers developed a procedure for the conversion of M. voltae cells into protoplasts that led to the release of S-layer protein into the protoplasting buffer medium (8). We grew M. voltae PS (DSM 1537) in a medium containing vitamin and mineral supplements under a gas atmosphere of 20% H2 and 80% CO2 at 37°C (13). Cells were taken from the logarithmic growth phase of the culture, and the protoplasts were prepared according to the method described by Patel and coworkers (8) with the modification that 2% NaCl replaced 0.34 M NaCl in the original cell suspension. After removal of the protoplasts by centrifugation, we found that the supernatant was highly enriched in S-layer protein, which we resolved on a one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gel (Fig.

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“…In spite of the S-layers robustness and the presence of precious cofactors, their industrial use in biotechnology and nutraceutics is strongly limited by the harsh conditions frequently required for their isolation and for the solubilization of their subunits (Nuβer and König 1987;Lin and Tan 2003). These facts lead to heterogeneity and partial destabilization which may imply the loss of monodispersity, an essential requirement to get a pure sample that may be subjected to a not expensive process of cofactor extraction or to a direct use for nanotechnologies.…”

Section: Discussionmentioning

confidence: 99%

“…As mentioned above, the industrial exploit of S-layer proteins is strongly limited by the harsh conditions required for their isolation and solubilization (Nuβer and König 1987;Lin and Tan 2003). In this work, we have modified the procedure to isolate one of the main S-layer proteins of D. radiodurans avoiding the use of strong detergents such as Sodium Dodecyl Sulphate and high temperatures (Baumeister et al 1982).…”

Section: Cell Walls Extrusion and Selective Isolation Of The Deinoxan...mentioning

confidence: 99%