scholarly journals Functional Characterization of Enzymatic Steps Involved in Pyruvylation of Bacterial Secondary Cell Wall Polymer Fragments

2018 ◽  
Vol 9 ◽  
Author(s):  
Fiona F. Hager ◽  
Arturo López-Guzmán ◽  
Simon Krauter ◽  
Markus Blaukopf ◽  
Mathias Polter ◽  
...  
Keyword(s):  
Cell Wall ◽  
Secondary Cell Wall ◽  
Functional Characterization ◽  
Cell Wall Polymer ◽  
Secondary Cell Wall Polymer

Structural characterization of the acid-degraded secondary cell wall polymer of Geobacillus stearothermophilus PV72/p2

2008 ◽  
Vol 343 (8) ◽  
pp. 1346-1358 ◽  
Author(s):  
Bent O. Petersen ◽  
Margit Sára ◽  
Christoph Mader ◽  
Harald F. Mayer ◽  
Uwe B. Sleytr ◽  
...  
Keyword(s):  
Cell Wall ◽  
Structural Characterization ◽  
Secondary Cell Wall ◽  
Geobacillus Stearothermophilus ◽  
Cell Wall Polymer ◽  
Secondary Cell Wall Polymer

scholarly journals High-Affinity Interaction between the S-Layer Protein SbsC and the Secondary Cell Wall Polymer of Geobacillus stearothermophilus ATCC 12980 Determined by Surface Plasmon Resonance Technology

2007 ◽  
Vol 189 (19) ◽  
pp. 7154-7158 ◽  
Author(s):  
Judith Ferner-Ortner ◽  
Christoph Mader ◽  
Nicola Ilk ◽  
Uwe B. Sleytr ◽  
Eva M. Egelseer
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Secondary Cell Wall ◽  
Geobacillus Stearothermophilus ◽  
Binding Behavior ◽  
Cell Wall Polymer ◽  
Secondary Cell Wall Polymer

ABSTRACT Surface plasmon resonance studies using C-terminal truncation forms of the S-layer protein SbsC (recombinant SbsC consisting of amino acids 31 to 270 [rSbsC31-270] and rSbsC31-443) and the secondary cell wall polymer (SCWP) isolated from Geobacillus stearothermophilus ATCC 12980 confirmed the exclusive responsibility of the N-terminal region comprising amino acids 31 to 270 for SCWP binding. Quantitative analyses indicated binding behavior demonstrating low, medium, and high affinities.

scholarly journals Structural and Functional Analyses of the Secondary Cell Wall Polymer of Bacillus sphaericus CCM 2177 That Serves as an S-Layer-Specific Anchor

1999 ◽  
Vol 181 (24) ◽  
pp. 7643-7646 ◽  
Author(s):  
Nicola Ilk ◽  
Paul Kosma ◽  
Michael Puchberger ◽  
Eva M. Egelseer ◽  
Harald F. Mayer ◽  
...  
Keyword(s):  
Cell Wall ◽  
Hydrofluoric Acid ◽  
Secondary Cell Wall ◽  
Bacillus Sphaericus ◽  
Nuclear Magnetic Resonance Analysis ◽  
Terminal Part ◽  
Resonance Analysis ◽  
Cell Wall Polymer ◽  
Functional Analyses ◽  
Secondary Cell Wall Polymer

ABSTRACT Sacculi of Bacillus sphaericus CCM 2177 contain a secondary cell wall polymer which was completely extracted with 48% hydrofluoric acid. Nuclear magnetic resonance analysis showed that the polymer is composed of repeating units, as follows: →3)-[4,6-O-(1-carboxyethylidene)]∼0.5-β-d-ManpNAc-(1→4)-β-d-GlcpNAc-(1→. The N-terminal part of the S-layer protein carrying S-layer homologous motifs recognizes this polymer as a binding site.

scholarly journals The S-Layer Proteins of Two Bacillus stearothermophilus Wild-Type Strains Are Bound via Their N-Terminal Region to a Secondary Cell Wall Polymer of Identical Chemical Composition

1998 ◽  
Vol 180 (6) ◽  
pp. 1488-1495 ◽  
Author(s):  
Eva Maria Egelseer ◽  
Karl Leitner ◽  
Marina Jarosch ◽  
Christoph Hotzy ◽  
Sonja Zayni ◽  
...  
Keyword(s):  
Cell Wall ◽  
Secondary Cell Wall ◽  
Bacillus Stearothermophilus ◽  
Proteolytic Cleavage ◽  
Terminal Region ◽  
Wild Type ◽  
Cell Wall Polymer ◽  
Secondary Cell Wall Polymer ◽  
Type Strains ◽  
Identical Chemical Composition

ABSTRACT Two Bacillus stearothermophilus wild-type strains were investigated regarding a common recognition and binding mechanism between the S-layer protein and the underlying cell envelope layer. The S-layer protein from B. stearothermophilusPV72/p6 has a molecular weight of 130,000 and assembles into a hexagonally ordered lattice. The S-layer from B. stearothermophilus ATCC 12980 shows oblique lattice symmetry and is composed of subunits with a molecular weight of 122,000. Immunoblotting, peptide mapping, N-terminal sequencing of the whole S-layer protein from B. stearothermophilus ATCC 12980 and of proteolytic cleavage fragments, and comparison with the S-layer protein from B. stearothermophilus PV72/p6 revealed that the two S-layer proteins have identical N-terminal regions but no other extended structurally homologous domains. In contrast to the heterogeneity observed for the S-layer proteins, the secondary cell wall polymer isolated from peptidoglycan-containing sacculi of the different strains showed identical chemical compositions and comparable molecular weights. The S-layer proteins could bind and recrystallize into the appropriate lattice type on native peptidoglycan-containing sacculi from both organisms but not on those extracted with hydrofluoric acid, leading to peptidoglycan of the A1γ chemotype. Affinity studies showed that only proteolytic cleavage fragments possessing the complete N terminus of the mature S-layer proteins recognized native peptidoglycan-containing sacculi as binding sites or could associate with the isolated secondary cell wall polymer, while proteolytic cleavage fragments missing the N-terminal region remained unbound. From the results obtained in this study, it can be concluded that S-layer proteins from B. stearothermophilus wild-type strains possess an identical N-terminal region which is responsible for anchoring the S-layer subunits to a secondary cell wall polymer of identical chemical composition.

The secondary cell wall polymer of Geobacillus tepidamans GS5-97T: structure of different glycoforms

2005 ◽  
Vol 340 (14) ◽  
pp. 2290-2296 ◽  
Author(s):  
Christian Steindl ◽  
Christina Schäffer ◽  
Vilko Smrečki ◽  
Paul Messner ◽  
Norbert Müller
Keyword(s):  
Cell Wall ◽  
Secondary Cell Wall ◽  
Cell Wall Polymer ◽  
Secondary Cell Wall Polymer

scholarly journals Influence of the Secondary Cell Wall Polymer on the Reassembly, Recrystallization, and Stability Properties of the S-Layer Protein from Bacillus stearothermophilus PV72/p2

1998 ◽  
Vol 180 (16) ◽  
pp. 4146-4153 ◽  
Author(s):  
Margit Sára ◽  
Christine Dekitsch ◽  
Harald F. Mayer ◽  
Eva M. Egelseer ◽  
Uwe B. Sleytr
Keyword(s):  
Cell Wall ◽  
Self Assembly ◽  
Secondary Cell Wall ◽  
Bacillus Stearothermophilus ◽  
Guanidine Hydrochloride ◽  
Terminal Region ◽  
Water Soluble ◽  
Outer Face ◽  
Cell Wall Polymer ◽  
Secondary Cell Wall Polymer

ABSTRACT The high-molecular-weight secondary cell wall polymer (SCWP) fromBacillus stearothermophilus PV72/p2 is mainly composed ofN-acetylglucosamine (GlcNAc) andN-acetylmannosamine (ManNAc) and is involved in anchoring the S-layer protein via its N-terminal region to the rigid cell wall layer. In addition to this binding function, the SCWP was found to inhibit the formation of self-assembly products during dialysis of the guanidine hydrochloride (GHCl)-extracted S-layer protein. The degree of assembly (DA; percent assembled from total S-layer protein) that could be achieved strongly depended on the amount of SCWP added to the GHCl-extracted S-layer protein and decreased from 90 to 10% when the concentration of the SCWP was increased from 10 to 120 μg/mg of S-layer protein. The SCWP kept the S-layer protein in the water-soluble state and favored its recrystallization on solid supports such as poly-l-lysine-coated electron microscopy grids. Derived from the orientation of the base vectors of the oblique S-layer lattice, the subunits had bound with their charge-neutral outer face, leaving the N-terminal region with the polymer binding domain exposed to the ambient environment. From cell wall fragments about half of the S-layer protein could be extracted with 1 M GlcNAc, indicating that the linkage type between the S-layer protein and the SCWP could be related to that of the lectin-polysaccharide type. Interestingly, GlcNAc had an effect on the in vitro self-assembly and recrystallization properties of the S-layer protein that was similar to that of the isolated SCWP. The SCWP generally enhanced the stability of the S-layer protein against endoproteinase Glu-C attack and specifically protected a potential cleavage site in position 138 of the mature S-layer protein.

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