I. Basic and applied S-layer research: an overview

Sleytr, Uwe B.

doi:10.1111/j.1574-6976.1997.tb00301.x

Cited by 107 publications

(92 citation statements)

References 57 publications

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“…Only the sequenced type strain C. glutamicum ATCC 13032 was devoid of the cspB gene along with a downstream ORF encoding a putative Zn-dependent alcohol dehydrogenase. It is a well-known phenomenon that bacteria can lose the ability for S-layer formation under specific culture conditions (Blaser et al, 1987;Fujimoto et al, 1989;Sleytr, 1997). In the present study, we demonstrated that C. glutamicum ATCC 13032 has apparently lost the ability for S-layer formation due to the chromosomal deletion of a 5?97 kb DNA region.…”

Section: Discussionsupporting

confidence: 53%

“…However, the loss of the S-layer locus might simply be the result of prolonged cultivation of the type-strain on synthetic medium since its discovery in 1957 and of its extensive use in the fermentation industry (Hermann, 2003;Sleytr & Sara, 1997). Thus, loss of the cspB gene region under favourable culture conditions might reflect a mechanism of deactivation of a non-required surface structure that is, moreover, synthesized in considerable amounts (Sleytr, 1997). Accordingly, it would be interesting to analyse original C. glutamicum ATCC 13032 isolates from the late 1950s for the presence of the cspB gene region.…”

Section: Discussionmentioning

confidence: 99%

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The surface (S)-layer gene cspB of Corynebacterium glutamicum is transcriptionally activated by a LuxR-type regulator and located on a 6 kb genomic island absent from the type strain ATCC 13032

et al. 2006

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The surface (S)-layer gene region of the Gram-positive bacterium Corynebacterium glutamicum ATCC 14067 was identified on fosmid clones, sequenced and compared with the genome sequence of C. glutamicum ATCC 13032, whose cell surface is devoid of an ordered S-layer lattice. A 5·97 kb DNA region that is absent from the C. glutamicum ATCC 13032 chromosome was identified. This region includes cspB, the structural gene encoding the S-layer protomer PS2, and six additional coding sequences. PCR experiments demonstrated that the respective DNA region is conserved in different C. glutamicum wild-type strains capable of S-layer formation. The DNA region is flanked by a 7 bp direct repeat, suggesting that illegitimate recombination might be responsible for gene loss in C. glutamicum ATCC 13032. Transfer of the cloned cspB gene restored the PS2− phenotype of C. glutamicum ATCC 13032, as confirmed by visualization of the PS2 proteins by SDS-PAGE and imaging of ordered hexagonal S-layer lattices on living C. glutamicum cells by atomic force microscopy. Furthermore, the promoter of the cspB gene was mapped by 5′ rapid amplification of cDNA ends PCR and the corresponding DNA fragment was used in DNA affinity purification assays. A 30 kDa protein specifically binding to the promoter region of the cspB gene was purified. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry and peptide mass fingerprinting of the purified protein led to the identification of the putative transcriptional regulator Cg2831, belonging to the LuxR regulatory protein family. Disruption of the cg2831 gene in C. glutamicum resulted in an almost complete loss of PS2 synthesis. These results suggested that Cg2831 is a transcriptional activator of cspB gene expression in C. glutamicum.

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Section: Discussionsupporting

confidence: 53%

Section: Discussionmentioning

confidence: 99%

The surface (S)-layer gene cspB of Corynebacterium glutamicum is transcriptionally activated by a LuxR-type regulator and located on a 6 kb genomic island absent from the type strain ATCC 13032

et al. 2006

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“…We can begin to answer this question through the intensive study of computer models inspired by real systems. A simple example of a natural hierarchical material is provided by the SbpA surface-layer (S-layer) protein, which forms a membrane on the outsides of the bacterium Lysinibacillus sphaericus and on surfaces in vitro [21][22][23][24] . This membrane, which is robust and controllably porous, is a square crystal lattice whose repeat unit is a tetramer, and so is a member of perhaps the simplest class of hierarchical materials, a one-component structure possessing order on two length scales (that of the monomer and that of the tetramer).…”

Section: Introductionmentioning

confidence: 99%

Do hierarchical structures assemble best via hierarchical pathways?

Haxton

Whitelam

2013

Soft Matter

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Hierarchically structured natural materials possess functionalities unattainable to the same components organized or mixed in simpler ways. For instance, the bones and teeth of mammals are far stronger and more durable than the mineral phases from which they are derived because their constituents are organized hierarchically from the molecular scale to the macroscale. Making similarly functional synthetic hierarchical materials will require an understanding of how to promote the self-assembly of structure on multiple lengthscales, without falling foul of numerous possible kinetic traps. Here we use computer simulation to study the self-assembly of a simple hierarchical structure, a square crystal lattice whose repeat unit is a tetramer. Although the target material is organized hierarchically, it self-assembles most reliably when its dynamic assembly pathway consists of the sequential addition of monomers to a single structure. Hierarchical dynamic pathways via dimer and tetramer intermediates are also viable modes of assembly, but result in general in lower yield: these intermediates have a stronger tendency than monomers to associate in ways not compatible with the target structure. In addition, assembly via tetramers results in a kinetic trap whereby material is sequestered in trimers that cannot combine to form the target crystal. We use analytic theory to relate dynamical pathways to the presence of equilibrium phases close in free energy to the target structure, and to identify the thermodynamic principles underpinning optimum self-assembly in this model: 1) make the free energy gap between the target phase and the most stable fluid phase of order k B T , and 2) ensure that no other dense phases (liquids or close-packed solids of monomers or oligomers) or fluids of incomplete building blocks fall within this gap.

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“…Structural differences might be found as a consequence of post-translational modifications such as glycosylation, transfer of phosphate and sulfate groups or proteolytic processing of the proteins (SÁRA and SLEYTR, 2000;SCHÄFER and MESSNER, 2001;SLEYTR, 1997). With a few exceptions, which include lac-tobacilli and the archaea Methanothermus fervidus and Methanothermus sociabilis (BRÖCKL et al, 1991), S-layer proteins have weakly acidic isoelectric points (SÁRA and SLEYTR, 2000;SLEYTR, 1997).…”

Section: Introductionmentioning

confidence: 99%

“…Depending on the growth conditions some microorganisms can also produce different surface proteins (BAUMEISTER and LEMBCKE, 1992;BEVERIDGE and KOVAL, 1993;BOOT and POUWELS, 1996;EGELSEER et al, 2001;KÖNIG and MESSNER, 1997;MESSNER and SLEYTR, 1992). Structural differences might be found as a consequence of post-translational modifications such as glycosylation, transfer of phosphate and sulfate groups or proteolytic processing of the proteins (SÁRA and SLEYTR, 2000;SCHÄFER and MESSNER, 2001;SLEYTR, 1997). With a few exceptions, which include lac-tobacilli and the archaea Methanothermus fervidus and Methanothermus sociabilis (BRÖCKL et al, 1991), S-layer proteins have weakly acidic isoelectric points (SÁRA and SLEYTR, 2000;SLEYTR, 1997).…”

Section: Introductionmentioning

confidence: 99%

Primary Structure of Selected Archaeal Mesophilic and Extremely Thermophilic Outer Surface Layer Proteins

Claus

Akça

Debaerdemaeker

et al. 2002

Systematic and Applied Microbiology

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SummaryThe archaea are recognized as a separate third domain of life together with the bacteria and eucarya. The archaea include the methanogens, extreme halophiles, thermoplasmas, sulfate reducers and sulfur metabolizing thermophiles, which thrive in different habitats such as anaerobic niches, salt lakes, and marine hydrothermals systems and continental solfataras. Many of these habitats represent extreme environments in respect to temperature, osmotic pressure and pH-values and remind on the conditions of the early earth. The cell envelope structures were one of the first biochemical characteristics of archaea studied in detail. The most common archaeal cell envelope is composed of a single crystalline protein or glycoprotein surface layer (S-layer), which is associated with the outside of the cytoplasmic membrane. The S-layers are directly exposed to the extreme environment and can not be stabilized by cellular components. Therefore, from comparative studies of mesophilic and extremely thermophilic S-layer proteins hints can be obtained about the molecular mechanisms of protein stabilization at high temperatures. First crystallization experiments of surface layer proteins under microgravity conditions were successful. Here, we report on the biochemical features of selected mesophilic and extremely archaeal S-layer (glyco-) proteins.

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I. Basic and applied S-layer research: an overview

Cited by 107 publications

References 57 publications

The surface (S)-layer gene cspB of Corynebacterium glutamicum is transcriptionally activated by a LuxR-type regulator and located on a 6 kb genomic island absent from the type strain ATCC 13032

The surface (S)-layer gene cspB of Corynebacterium glutamicum is transcriptionally activated by a LuxR-type regulator and located on a 6 kb genomic island absent from the type strain ATCC 13032

Do hierarchical structures assemble best via hierarchical pathways?

Primary Structure of Selected Archaeal Mesophilic and Extremely Thermophilic Outer Surface Layer Proteins

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