The Occurrence of Bactoprenol in the Mesosome and Plasma Membranes of Lactobacillus casei and Lactobacillus plantarum

Thorne, Kareen J. I.; Barker, Douglas C.

doi:10.1099/00221287-70-1-87

Cited by 21 publications

(10 citation statements)

References 42 publications

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“…Recently, freezeetching has also been used successfully to reveal the same regularly ordered array of the cell wall in some gram-positive bacteria [10,23]. Although the ultrastructure of some lactobacilli was extensively studied by electron microscopy of thin sections [3,12,27], little is known of the freeze-etched structure of the organisms. Higgins et al [9] demonstrated in freeze-fractured cells of Lactobacillus acidophilus that the cell wall ap peared to be a homogeneous layer with a fairly smooth outer surface.…”

Section: Discussionmentioning

confidence: 99%

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Regular Array in the Cell Wall of Lactobacillus fermenti as Revealed by Freeze‐Etching and Negative Staining1

Kawata

Masuda

Yoshino

et al. 1974

Japanese Journal of Microbiology

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Freeze-etching of Lactobacillus fermenti F-4 (NCTC 7230) revealed that the outer layer of the cell wall was composed of a regular array in which parallel lines ran obliquely to the longitudinal axis of the cell with an average distance between the centers of about 9.6 nm and were intersected by thinner lines with an average periodicity of approximately 6.2 nm at an angle of about 75 °. Occasionally the direction of the striation was discontinuously shifted near one end of the cell. Beneath the regular array the middle cell wall layer packed with granules and the smooth inner cell wall layer were discernible and the meso somes were also visible in the cytoplasm. When the ultrastructure of isolated outer cell wall fragments was examined by negative staining, the regular array appeared to be composed of subunits, about 3.6 nm in diameter, which were arranged in a tetragonal pattern. The tetragonal array consisted of the subunits in rows in two directions at an angle of about 75 ° to each other.The average spacing be tween the rows was about 9.3 nm in one direction and 5.5 nm in the other direction.

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Section: Discussionmentioning

confidence: 99%

“…Several investigators demonstrated both vesicular and lamellar mesosomes in freeze etched gram-positive bacteria [10,16,17]. The mesosome of lactobacilli was found in thin sections [3,12,27]. Figure 4 shows an oblique-fractured face of the cytoplasm.…”

Section: Freeze-etched Cellsmentioning

confidence: 99%

Regular Array in the Cell Wall of Lactobacillus fermenti as Revealed by Freeze‐Etching and Negative Staining1

Kawata

Masuda

Yoshino

et al. 1974

Japanese Journal of Microbiology

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“…Recent studies by Frehel et al (118) demonstrate that deposits of tellurite, which are reliable cytological indicators of respiratory activity, are scattered over the plasma membrane but never occur on the mesosomes. Moreover, isolated mesosomes are deficient in NADH oxidase, succinic dehydrogenase, AT-Pase, and cytochromes (94,107,312,365,366). The evidence that mesosomes are involved in cell division, circumstantial as it is, carries more conviction.…”

Section: Structural Basismentioning

confidence: 99%

Conservation and transformation of energy by bacterial membranes.

Harold¹

1972

Bacteriological Reviews

433

174

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“…There have been two biochemical findings by which involvement of the mesosomes in peptidoglycan synthesis is taken into account; (i) mesosomes contain bactoprenol, an intermediate carrier in peptidoglycan synthesis, in Lactobacillus casei and L. plantarum (39), and (ii) mesosomes have higher autolytic activity than cytoplasmic membranes in M. luteus (28). PBPs function in the synthesis and organization of peptidoglycan during cell growth and division (37).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Mesosomes of Micrococcus luteus: Isolation and Properties of Mesosomal Ribosomes, and Localization of Penicillin‐Binding Proteins in Mesosomal Membranes

Nakasone¹,

Masuda²,

Kawata³

1987

Microbiology and Immunology

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Mesosomes were isolated and purified from Micrococcus luteus under hypertonic conditions throughout preparation processes. The purified mesosomal preparation was composed of closed tubules and vesicles. Electron-dense ribosomelike particles were observed within the isolated mesosomal vesicles by electron microscopy. The ribosome-like particles were isolated from the purified mesosomes by a procedure involving solubilization of the membranes with detergents followed by centrifugation on a linear density gradient of sucrose. The isolated particles have a sedimentation coefficient of 70S in the presence of 10 MM Mg2+, when Mg2+ concentration was lowered to 0.1 mM, the particles were dissociated into two sub-particles of 30S and 50S. The 70S particles had the same appearance as cytoplasmic 70S ribosome particles upon observations of negatively stained preparations. These findings indicate that mesosomal tubules contain ribosomes. The isolated mesosomal ribosomes had the ability for protein synthesis when polyuridylic acid-directed polyphenylalanine synthesis was assayed. The sensitivity of mesosomal ribosomes to inhibitors, chloramphenicol and streptomycin, for protein synthesis was significantly lower than that of both cytoplasmic and cytoplasmic membrane-bound ribosomes. In addition, three penicillin-binding proteins were detected in the mesosomal membranes. One of these was localized predominantly in the mesosomal membranes and the other two were distributed almost equally in both mesosomal and cytoplasmic membranes.

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The Occurrence of Bactoprenol in the Mesosome and Plasma Membranes of Lactobacillus casei and Lactobacillus plantarum

Cited by 21 publications

References 42 publications

Regular Array in the Cell Wall of Lactobacillus fermenti as Revealed by Freeze‐Etching and Negative Staining1

Regular Array in the Cell Wall of Lactobacillus fermenti as Revealed by Freeze‐Etching and Negative Staining1

Conservation and transformation of energy by bacterial membranes.

Characterization of Mesosomes of Micrococcus luteus: Isolation and Properties of Mesosomal Ribosomes, and Localization of Penicillin‐Binding Proteins in Mesosomal Membranes

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