The high‐molecular‐mass amylase (HMMA) of <i>Geobacillus stearothermophilus</i> ATCC 12980 interacts with the cell wall components by virtue of three specific binding regions

Ferner-Ortner-Bleckmann, Judith; Huber-Gries, Carina; Pavkov, Tea; Keller, Walter; Mader, Christoph; Ilk, Nicola; Sleytr, Uwe B.; Egelseer, Eva M.

doi:10.1111/j.1365-2958.2009.06734.x

Cited by 15 publications

(12 citation statements)

References 51 publications

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“…Using heterologously produced N‐ or C‐terminally truncated SbsC forms and the native HMMA for affinity studies, it turned out that the N‐terminal part of SbsC must comprise the binding region for the exoenzyme (Jarosch et al ., ). After elucidation of the hmma gene sequence, the full‐length rHMMA, N‐ or C‐terminal rHMMA truncations, as well as C‐terminal rHMMA fragments were heterologously produced (Ferner‐Ortner‐Bleckmann et al ., ). The different rHMMA forms were used either for affinity studies with rSbsC, peptidoglycan‐containing sacculi, and pure peptidoglycan devoid of SCWP, or for SPR studies using rSbsC 31‐443 (a truncated rSbsC form comprising the N‐terminus) and isolated SCWP.…”

Section: Functional Aspectsmentioning

confidence: 97%

“…The different rHMMA forms were used either for affinity studies with rSbsC, peptidoglycan‐containing sacculi, and pure peptidoglycan devoid of SCWP, or for SPR studies using rSbsC 31‐443 (a truncated rSbsC form comprising the N‐terminus) and isolated SCWP. On the basis of all available data, a specific binding region for each of the three cell wall components (rSbsC, SCWP, and peptidoglycan) could be identified in the C‐terminal part of the rHMMA, representing the smallest regions necessary for interaction (Ferner‐Ortner‐Bleckmann et al ., ).…”

Section: Functional Aspectsmentioning

confidence: 97%

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S-layers: principles and applications

et al. 2014

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Monomolecular arrays of protein or glycoprotein subunits forming surface layers (S-layers) are one of the most commonly observed prokaryotic cell envelope components. S-layers are generally the most abundantly expressed proteins, have been observed in species of nearly every taxonomical group of walled bacteria, and represent an almost universal feature of archaeal envelopes. The isoporous lattices completely covering the cell surface provide organisms with various selection advantages including functioning as protective coats, molecular sieves and ion traps, as structures involved in surface recognition and cell adhesion, and as antifouling layers. S-layers are also identified to contribute to virulence when present as a structural component of pathogens. In Archaea, most of which possess S-layers as exclusive wall component, they are involved in determining cell shape and cell division. Studies on structure, chemistry, genetics, assembly, function, and evolutionary relationship of S-layers revealed considerable application potential in (nano)biotechnology, biomimetics, biomedicine, and synthetic biology.

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Section: Functional Aspectsmentioning

confidence: 97%

Section: Functional Aspectsmentioning

confidence: 97%

S-layers: principles and applications

et al. 2014

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“…SLH domains 50 to 60 amino acids (aa) long have been identified at the aminoterminal region of S-layer proteins from various organisms (45) and at the carboxy-terminal end of cell-associated extracellular enzymes (45,47). S-layer motifs specifically recognize pyruvylated secondary cell wall polymers (SCWPs) as the anchoring structure (17,47). SLH domains seemingly play a contributing role in plant polysaccharide degradation.…”

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confidence: 99%

S-Layer Homology Domain Proteins Csac_0678 and Csac_2722 Are Implicated in Plant Polysaccharide Deconstruction by the Extremely Thermophilic Bacterium Caldicellulosiruptor saccharolyticus

Ozdemir

Blumer-Schuette

Kelly

2012

Appl Environ Microbiol

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The genus Caldicellulosiruptor contains extremely thermophilic bacteria that grow on plant polysaccharides. The genomes of Caldicellulosiruptor species reveal certain surface layer homology (SLH) domain proteins that have distinguishing features, pointing to a role in lignocellulose deconstruction. Two of these proteins in Caldicellulosiruptor saccharolyticus (Csac_0678 and Csac_2722) were examined from this perspective. In addition to three contiguous SLH domains, the Csac_0678 gene encodes a glycoside hydrolase family 5 (GH5) catalytic domain and a family 28 carbohydrate-binding module (CBM); orthologs to Csac_0678 could be identified in all genome-sequenced Caldicellulosiruptor species. Recombinant Csac_0678 was optimally active at 75°C and pH 5.0, exhibiting both endoglucanase and xylanase activities. SLH domain removal did not impact Csac_0678 GH activity, but deletion of the CBM28 domain eliminated binding to crystalline cellulose and rendered the enzyme inactive on this substrate. Csac_2722 is the largest open reading frame (ORF) in the C. saccharolyticus genome (predicted molecular mass of 286,516 kDa) and contains two putative sugar-binding domains, two Big4 domains (bacterial domains with an immunoglobulin [Ig]-like fold), and a cadherin-like (Cd) domain. Recombinant Csac_2722, lacking the SLH and Cd domains, bound to cellulose and had detectable carboxymethylcellulose (CMC) hydrolytic activity. Antibodies directed against Csac_0678 and Csac_2722 confirmed that these proteins bound to the C. saccharolyticus S-layer. Their cellular localization and functional biochemical properties indicate roles for Csac_0678 and Csac_2722 in recruitment and hydrolysis of complex polysaccharides and the deconstruction of lignocellulosic biomass. Furthermore, these results suggest that related SLH domain proteins in other Caldicellulosiruptor genomes may also be important contributors to plant biomass utilization.

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“…These methodologies involve an ultrasensitive mass sensor that monitors real time changes in the adsorbed amount of material. They allow the investigation of the mechanisms of recrystallization of SLPs at a nanoscale level and therefore it is important for understanding and engineering of biomembranes and biosensors [110]. QCM has for instance been used to follow in situ the self-assembly of SLPs from solution to solid substrates on gold or SiO 2 surfaces [111] and also used to investigate in situ the electrochemical behavior of the SLPs on gold electrodes with the capability to measure mass changes at the nanogram level at the electrode surface/electrolyte interfaces [94,112,113].…”

Section: Quartz Crystal Microbalance and Surface Plasmon Resonancementioning

confidence: 99%

Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction

Mobili

2013

IJBCRR

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Surface-layers (S-layers) are macromolecular paracrystalline arrays of proteins or glycoproteins that can self-assemble into 2-dimensional semi-permeable meshworks to overlay the cell surface of many bacteria and archaea. They usually assemble into lattices with oblique, square or hexagonal symmetry and serve as an interface between the bacterial cell and the environment. Isolated S-layers can recrystallize into two-dimensional regular arrays in suspension or on various surfaces, thus being an appropriate material for several bionanotechnological purposes. Promising applications of S-layers include their use as biotemplates for the capture of metal ions or the synthesis of metal nanoclusters. Research ArticleInternational Journal of Biochemistry Research & Review, 3(1): 39-62, 2013 40 Considering the use of S-layers as biotemplates for the organization of metal ions or metallic nanoclusters, research on potential of surface layer proteins (SLP) and metals can be understood as an interdisciplinary field, in which different biophysical techniques supply complementary information. In this review, we discuss the SLP as native or engineered "bottom-up" building blocks for metal immobilization structures. We also describe the biophysical techniques used to analyze metal binding properties as well as the information obtained from the investigation of these structures.

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The high‐molecular‐mass amylase (HMMA) of Geobacillus stearothermophilus ATCC 12980 interacts with the cell wall components by virtue of three specific binding regions

Cited by 15 publications

References 51 publications

S-layers: principles and applications

S-layers: principles and applications

S-Layer Homology Domain Proteins Csac_0678 and Csac_2722 Are Implicated in Plant Polysaccharide Deconstruction by the Extremely Thermophilic Bacterium Caldicellulosiruptor saccharolyticus

Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction

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