Crystalline surface layers in procaryotes

Sleytr, Uwe B.; Messner, Paul

doi:10.1128/jb.170.7.2891-2897.1988

Cited by 217 publications

(140 citation statements)

References 100 publications

(110 reference statements)

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“…The PAGE experiments involving prolonged denaturation times suggested that the 52 kDa protein might be a trimer involving disulphide bridges between 17 kDa monomers. Such associations of cell wall proteins have been observed in other Gram-positive bacteria (Sleytr & Messner, 1988). The assignment of peptidoglycan mostly to the inner cell wall layer was substantiated by several observations.…”

Section: Discussionsupporting

confidence: 55%

Cell wall and autolytic system of Lactobacillus helveticus ATCC 12046

Lortal¹,

Rousseau

Boyaval³

et al. 1991

Journal of General Microbiology

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The cell wall of Lactobacillus helveticus was found to have a three-layered structure when thin sections of whole cells or isolated cell walls were stained by various procedures and examined by electron microscopy. The main feature of the composition of isolated cell walls was a high protein content (about 48% of the cell wall dry weight) with a predominant 52 kDa protein. Peptidoglycan and what was considered as teichoic acids accounted for 36% and 14%, respectively, of the cell wall dry weight. The 52 kDa protein was apparently unglycosylated, located in the outer layer and noncovalently bound to the inner layers. Peptidoglycan was mostly assigned to the innermost layer. The conditions leading to autolysis of whole cells or isolated cell walls were determined, as well as the specificity of the autolysin involved in cell wall degradation. IntroductionLactobacillus helveticus is an important lactic acid bacterium that is involved in cheese technology (Accolas et al., 1980;Turner et al., 1983) and that has recently become the object of interest for genetic manipulation (Chassy, 1987;Sandine, 1987;Thomas & Collins, 1988). Its autolysis with the concomitant release of cytoplasmic proteases (Ezzat et al., 1986) is an essential feature of cheese maturation (Bie & Sjostrom, 1975a, b). A better understanding of the autolytic system of L. helveticus could perhaps offer a new way for an accelerated ripening of cheese. Ohmiya & Sat0 (1970) were the first to follow the autolysis of L. helveticus in technological conditions. After adding whole cells to an aseptic rennet curd, the release of DNA was noted and autolysed cells were clearly observed by electron microscopy. More recently, we promoted the autolysis of L. helveticus by suspending whole cells in dilute buffers (Lortal et al., 1989). A clear understanding of the autolytic system of L. helveticus implies, in particular, a better knowledge of the composition and structure of its cell wall, which have so far been investigated only to a limited extent (Ikawa & Snell, 1960;Baddiley & Davison, 1961 ; Williams, 1971). The main peptidoglycan amino acids were determined (Glu, Ala, Asp, Lys) as well as their respective percentage in the D-configuration (Ikawa & Snell, 1960). Previous studies also revealed the presence of glyceroltype teichoic acids (Baddiley & Davison, 1961) and neutral sugars (glucose, galactose but no rhamnose). Wall and membrane teichoic acids of L. helveticus were shown to have antigenic properties (Knox & Wicken, 1971). It has also been suggested that the cell wall of L. helveticus ATCC 10797 was composed of two layers with the outer layer presumably containing a predominant protein (Masuda & Kawata, 1983).In the work described here, a more detailed investigation of the morphology and composition of the cell wall of L. helveticus ATCC 12046 was undertaken. Moreover, the main characteristics of the autolytic system of this strain were investigated, in particular ways of promoting lysis, the effect of external factors, and the specificity of the autolytic...

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Section: Discussionsupporting

confidence: 55%

Cell wall and autolytic system of Lactobacillus helveticus ATCC 12046

Lortal¹,

Rousseau

Boyaval³

et al. 1991

Journal of General Microbiology

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“…Gram-positive bacteria lack the outer membrane (and LPS), but the peptidoglycan layer is usually much thicker. Many eubacteria and archaea are also surrounded by a proteinaceous crystalline surface layer (S-layer) which then forms the outermost component of the cell envelope [2]. The outer membrane of Gram-negative bacteria functions as a molecular sieve through which molecules with a molecular mass > 600-1000 Da cannot penetrate, and the hydrophilic LPS layer may form a barrier for lipophilic compounds [1,3].…”

Section: General Introductionmentioning

confidence: 99%

Secondary solute transport in bacteria

Poolman

Konings

1993

Biochimica et Biophysica Acta (BBA) - Bioenergetics

202

160

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“…Electrostatic forces are responsible for the attachment of Bacilltls stlbtilis cell-wall-bound proteins (CWBPs) (Studer, 1988), while the linkage of Staph_ylococctl.r atlretls protein A to PG is covalent (Schneewind e t al., 1990). Frequently, proteinaceous paracrystalline S-layers are present at the outer surface of the wall (Sleytr & Messner, 1988).…”

Section: Introductionmentioning

confidence: 99%

The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease

Margot¹,

Karamata²

1996

Microbiology

100

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The nucleotide sequence of wprA, a protease-encoding gene of Bacillus subtilis 168, is reported. The gene, expressed during the exponential growth phase, belongs to a monocistronic operon. WprA is a 96 kDa polypeptide endowed with a signal peptide, as well as a propeptide. Upon processing and export, it gives rise to two previously identified cell-wall-bound proteins, CWBP23 and 52. Processing of WprA exhibits a novel feature of protein export, whereby removal of the middle part of the molecule accompanies the targeting to the cell wall of its N-and C-terminal parts, which correspond to CWBP23 and 52, respectively. Sequence analyses and enzymic assays reveal that CWBP52 is a serine protease. Growth rate, cell morphology, sporulation and motility of wprA mutants apparently do not differ from those of the parent strain.

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Crystalline surface layers in procaryotes

Cited by 217 publications

References 100 publications

Cell wall and autolytic system of Lactobacillus helveticus ATCC 12046

Cell wall and autolytic system of Lactobacillus helveticus ATCC 12046

Secondary solute transport in bacteria

The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease

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