Characterization of mesosomes of Micrococcus luteus: isolation and properties of mesosomal ribosomes, and localization of penicillin-binding proteins in mesosomal membranes.
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 ribosome-like 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.
Nakasone
N
N
Department of Food Microbiology, Tokushima University School of Medicine.
Masuda
K
K
Kawata
T
T
D001426:Bacterial Proteins / Q000096:biosynthesis; D002352:Carrier Proteins / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D002701:Chloramphenicol / Q000494:pharmacology; D003513:Cycloheximide / Q000494:pharmacology; D006602:Hexosyltransferases; D007425:Intracellular Membranes / Q000032:analysis*; D008837:Micrococcus / Q000032:analysis / Q000648:ultrastructure*; D008854:Microscopy, Electron; D002267:Muramoylpentapeptide Carboxypeptidase / Q000032:analysis*; D009940:Organoids / Q000032:analysis / Q000648:ultrastructure*; D046915:Penicillin-Binding Proteins; D010452:Peptide Biosynthesis; D010455:Peptides; D010458:Peptidyl Transferases; D012270:Ribosomes / Q000032:analysis* / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D013307:Streptomycin / Q000494:pharmacology
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010455:Peptides; C012001:polyphenylalanine; D002701:Chloramphenicol; D003513:Cycloheximide; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D013307:Streptomycin