The diacetamidodideoxyuronic-acid-containing glycan chain of Bacillus stearothermophilus NRS 2004/3a represents the secondary cell-wall polymer of wild-type B. stearothermophilus strains

Schäffer, Christina; Kählig, Hanspeter; Christian, Rudolf; Schulz, Gerhard; Zayni, Sonja; Messner, Paul

doi:10.1099/13500872-145-7-1575

Cited by 60 publications

(45 citation statements)

References 9 publications

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“…Nevertheless, the N-terminal part of the S-layer proteins of B. stearothermophilus wild-type strains is highly conserved and recognizes a net negatively charged secondary cell wall polymer as the binding site (35,53). This type of secondary cell wall polymer is composed of tetrasaccharide repeating units that contain glucose, N-acetylglucosamine, and 2,3-diacetamido-2,3-dideoxymannuronic acid in a molar ratio of 1 to 1 to 2 (117). Sequence analysis of the S-layer proteins from B. stearothermophilus PV72/p6 and ATCC 12980 (Table 1) revealed an accumulation of arginine, lysine, and tyrosine at the N-terminal part.…”

Section: Attachment Of S-layer Proteins To the Underlying Cell Envelomentioning

confidence: 99%

S-Layer Proteins

2000

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Section: Attachment Of S-layer Proteins To the Underlying Cell Envelomentioning

confidence: 99%

S-Layer Proteins

2000

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“…The SCWPs of B. stearothermophilus PV72\p6, ATCC 12980 and NRS 2004\3a have an identical chemical composition, which led to the conclusion that this type of SCWP might be typical of B. stearothermophilus wild-type strains (Egelseer et al, 1998). More recently, the complete structure was provided by NMR analysis, showing that this type of SCWP is composed of repeating units that contain glucose, Nacetylglucosamine and 2,3-diacetamido-2,3-dideoxy--mannuronic acid in a molar ratio of 1 to 1 to 2 (Scha$ ffer et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

S-layer gene sbsC of Bacillus stearothermophilus ATCC 12980: molecular characterization and heterologous expression in Escherichia coli The GenBank accession number for the sequence described in this paper is AF055578.

Jarosch

Egelseer

Mattanovich³

et al. 2000

Microbiology

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The cell surface of Bacillus stearothermophilus ATCC 12980 is completely covered with an oblique S-layer lattice. To investigate sequence identities and a common structure-function relationship in S-layer proteins of different B. stearothermophilus wild-type strains, the nucleotide sequence encoding the S-layer protein SbsC of B. stearothermophilus ATCC 12980 was determined by PCR techniques. The entire sbsC sequence showed an ORF of 3297 bp predicted to encode a protein of 1099 aa with a theoretical molecular mass of 115 409 Da and an isoelectric point of 573. Primer extension analysis suggested the existence of two promoter regions. Amino acid sequence comparison between SbsC and SbsA, a previously characterized S-layer protein of B. stearothermophilus PV72/p6 which assembles into a hexagonally ordered lattice, revealed an identical secretion signal peptide, 85 % identity for the N-terminal regions (aa 31-270) which do not carry any S-layer homologous motifs, but only 21 % identity for the rest of the sequences. Affinity studies demonstrated that the N-terminal part of SbsC is necessary for recognition of a secondary cell wall polymer. This was in accordance with results obtained in a previous study for SbsA, thus confirming a common functional principle for the N-terminal parts of both S-layer proteins. The sbsC coding region cloned into the pET3a vector without its own upstream region, the signal sequence and the 3' transcriptional terminator led to stable expression in Escherichia coli.

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“…At least for S-layer proteins of Bacillaceae, the N-terminal region was found to be responsible for anchoring the S-layer subunits to the underlying rigid cell envelope layer by binding to a heteropolysaccharide termed the secondary cell wall polymer (SCWP) (19,21,24). In Bacillaceae, at least two types of mechanisms for the binding of S-layer proteins and SCWPs have been identified.…”

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“…The second type of binding mechanism for S-layer proteins and SCWPs has been identified in the G. stearothermophilus wild-type strains PV72/p6, NRS 2004/3a, and ATCC 12980 (6,11,12,24,25), as well as a temperature-derived strain variant of the latter (5). G. stearothermophilus ATCC 12980 produces the S-layer protein SbsC, the subject of the study described here.…”

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confidence: 99%