High-molecular-weight penicillin-binding proteins from membranes of bacilli
نویسندگان
چکیده
منابع مشابه
Synthesis of peptidoglycan by high molecular weight penicillin-binding proteins of Bacillus subtilis and Bacillus stearothermophilus.
The high molecular weight penicillin-binding proteins (PBP(s) ) Bacillus subtilis PBPs 1, 2, and 4 and Bacillus stearothermophilus PBPs 1-4 were shown to catalyze peptidoglycan synthesis from the undecaprenol-containing lipid intermediate substrate in two assay systems. In a filter paper assay system, high levels of substrate polymerization occurred when reaction mixtures were incubated on What...
متن کاملStudies of the high molecular weight penicillin-binding proteins of Bacillus subtilis.
Seven or eight penicillin-binding proteins (PBPs) were detected in Bacillus subtilis membranes. By introducing covalent affinity chromatography employing cephalosporins as ligands, milligram amounts of three high molecular weight PBPs (PBP 1 ab, Mr = 120,000; PBP 2b, Mr = 94,000; and PBP 4, Mr = 78,000) were obtained without any contamination of the major PBP 5, the D-alanine carboxypeptidase. ...
متن کاملStudies of the High Molecular Weight Penicillin-binding Proteins of Bacillus subtiEs*
Seven or eight penicillin-binding proteins (PBPs) were detected in Bacillus subtilis membranes. By introducing covalent affinity chromatography employing cephalosporins as ligands, milligram amounts of three high molecular weight PBPs (PBP 1 ab, M, = 120,000; PBP 2b, M, = 94,000; and PBP 4, M, = 78,000) were obtained without any contamination of the major PBP 5, the D-alanine carboxypeptidase. ...
متن کاملPhenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular-weight penicillin-binding proteins.
Examination of Bacillus subtilis strains containing multiple mutations affecting the class A high-molecular-weight penicillin-binding proteins (PBPs) 1, 2c, and 4 revealed a significant degree of redundancy in the functions of these three proteins. In rich media, loss of PBPs 2c and 4 resulted in no obvious phenotype. The slight growth and cell morphology defects associated with loss of PBP 1 w...
متن کاملTwo class A high-molecular-weight penicillin-binding proteins of Bacillus subtilis play redundant roles in sporulation.
The four class A penicillin-binding proteins (PBPs) of Bacillus subtilis appear to play functionally redundant roles in polymerizing the peptidoglycan (PG) strands of the vegetative-cell and spore walls. The ywhE product was shown to bind penicillin, so the gene and gene product were renamed pbpG and PBP2d, respectively. Construction of mutant strains lacking multiple class A PBPs revealed that...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1981
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.148.3.950-955.1981