Three-dimensional structure of the regular surface glycoprotein layer of <i>Halobacterium volcanii</i>
 from the Dead Sea

Kessel, Martin; Wildhaber, Ivo; Cohen, S.; Baumeister, Wolfgang

doi:10.1002/j.1460-2075.1988.tb02974.x

Cited by 76 publications

(64 citation statements)

References 22 publications

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“…For example, iduronic acid, a major component of proteoglycans (296), is found in the glycans decorating the Halobacterium salinarum S-layer glycoprotein. Similarly, the O-glycosylation cluster situated near the membrane-spanning base of the Haloferax volcanii S-layer glycoprotein has also been assigned a structural support role in the formation of a periplasmic-like space (217). In Thermoplasma acidophilum, an organism that lacks a cell wall, it has been suggested that the glycan moieties attached to the major glycosylated membrane-bound protein species coating the cell surface act to either trap water molecules or allow the cell surface proteins to interact with each other.…”

Section: Role Of Protein Glycosylation In Archaeamentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review

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Section: Role Of Protein Glycosylation In Archaeamentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

196

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“…The main component of the cell wall is the S-layer formed by a hexagonal arrangement of a glycoprotein (25). A detailed structural study of the S-layer of H. volcanii (26) together with a a previous x-ray study of the envelope of H. halobium (27) led to a model in which the upper external part of the glycoprotein forms a dome-shaped region separated from the cell membrane by spacer elements (26). The protein is thought to be anchored in the plasma membrane by a hydrophobic stretch that is observed near the C terminus of both the H. halobium and H. volcanii glycoprotein sequence (28,29).…”

Section: Resultsmentioning

confidence: 99%

“…The protein is thought to be anchored in the plasma membrane by a hydrophobic stretch that is observed near the C terminus of both the H. halobium and H. volcanii glycoprotein sequence (28,29). The interspace between the plasma membrane and the external part of the S-layer has been considered as an aqueous space analogous to the periplasm of Gram-negative bacteria (26,27). However, if porins are present in the cell wall, but do not belong to the plasma membrane, they should be located in this interspace, which should then contain a lipid membrane.…”

Section: Resultsmentioning

confidence: 99%

Voltage-dependent Porin-like Ion Channels in the Archaeon Haloferax volcanii

Besnard

Martinac

Ghazi

1997

Journal of Biological Chemistry

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Membrane vesicles isolated from the cell envelope of the archaebacterium Haloferax volcanii were either reconstituted in giant liposomes and examined by the patch-clamp technique or were fused into planar lipid bilayers. In addition, cell envelope proteins were solubilized by detergent and reconstituted in azolectin liposomes, which were then fused into planar lipid bilayers. Independently of the technique used the predominant channel activity encountered exhibited the following characteristics. Channels were open at all voltages in the range approximately ؊120 to ؉120 mV and exhibited frequent fast transitions to closed levels of different amplitudes. At voltages greater than 120 mV the channels tended to close in a manner characterized by large, slow transitions of variable amplitudes. The tendency to close at high membrane potentials was much stronger at one polarity. The channel gating pattern was complex exhibiting a range of subconductances of 10 -300 picosiemens in symmetric 100 mM KCl. These electrophysiological characteristics are comparable with those of bacterial and mitochondrial porins, suggesting that the archaeal channels may belong to the general class of porin channels. Some channels showed preference for K ؉ , whereas the others preferred Cl ؊ , suggesting the existence of at least two types of porin-like channels in H. volcanii.

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“…Similar results were obtained by Walker et al (1994), who proposed that the S-layer proteins of Caulobacter crescentus interact with lipopolysaccharide via calcium bridges. Finally, in the case of halobacteria, a short C-terminal hydrophobic sequence has been identified and proposed to be a cytoplasmic transmembrane anchoring sequence for the S-layer protein (Lechner and Sumper, 1987;Kessel et al, 1988;Sumper et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

**The S‐layer protein of Corynebacterium glutamicum is anchored to the cell wall by its C‐terminal hydrophobic domain**

Chami

Bayan

Peyret

et al. 1997

Molecular Microbiology

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SummaryPS2 is the S-layer protein of Corynebacterium glutamicum. The S-layer may be detached from the cell as organized sheets by detergents at room temperature. The solubilization of PS2 in the form of monomers requires detergent treatment at high temperature (70ЊC), conditions under which the protein is denatured. Treatment of the cells with proteinase K or trypsin results in the detachment of the organized S-layer, which remains organized. Because we show that trypsin cleaves the C-terminal part of the protein, we conclude that this domain is involved in the association of the S-layer to the cell but is not essential in the interaction between individual PS2 proteins within the S-layer. A modified form of PS2, deleted of its C-terminal hydrophobic sequence, was constructed. The protein is almost unable to form an organized S-layer and is mainly released into the medium. We suggest that PS2 is anchored via its C-terminal hydrophobic sequence to a hydrophobic layer of the wall of the bacterium located some distance above the cytoplasmic membrane.

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Three-dimensional structure of the regular surface glycoprotein layer of Halobacterium volcanii from the Dead Sea

Cited by 76 publications

References 22 publications

Posttranslational Protein Modification inArchaea

Posttranslational Protein Modification inArchaea

Voltage-dependent Porin-like Ion Channels in the Archaeon Haloferax volcanii

**The S‐layer protein of Corynebacterium glutamicum is anchored to the cell wall by its C‐terminal hydrophobic domain**

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