Dispensability of either penicillin-binding protein -1a or -1b involved in the essential process for cell elongation in Escherichia coli
| Autor: | Jun-ichi Kato, Hideho Suzuki, Yukinori Hirota |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Penicillin binding proteins
Muramoylpentapeptide Carboxypeptidase Biology medicine.disease_cause Coliphages Nucleic acid thermodynamics chemistry.chemical_compound Muramoylpentapeptide carboxypeptidase Plasmid Bacterial Proteins Multienzyme Complexes Escherichia coli Genetics medicine Penicillin-Binding Proteins Molecular Biology Gene Strain (chemistry) Nucleic Acid Hybridization DNA Restriction Enzymes Molecular biology Genes Hexosyltransferases chemistry Genes Bacterial Peptidyl Transferases Carrier Proteins Acyltransferases Nutrient agar Plasmids |
| Zdroj: | Molecular and General Genetics MGG. 200:272-277 |
| ISSN: | 1432-1874 0026-8925 |
| DOI: | 10.1007/bf00425435 |
| Popis: | A strain of Escherichia coli lacking the entire ponB gene and a strain lacking the proximal part of the ponA gene were constructed by substitution with a drug resistance gene. These strains lost either penicillin-binding protein(PBP)-1b or -1a totally and their growth was apparently normal at 30 degrees C and 42 degrees C except that growth of the ponB deletion strain was poor on a nutrient agar plate containing no NaCl at 30 degrees C as well as at 42 degrees C. Transductional experiments to introduce the ponB deletion into the ponA deletion strain, and vice versa, showed that the ponA ponB double deletion was lethal unless the deletion was functionally compensated, e.g., by the presence of a plasmid carrying either gene. Thus, either PBP-1b (ponB) or PBP-1a (ponA), but not both, is dispensable for cell viability, at least under ordinary culture conditions. Transductional experiments also suggested that the gamma component of PBP-1b or the PBP-1b lacking the C-terminal portion encoded in the distal region to the SphI site on the ponB was sufficient for supporting growth of the E. coli cell. |
| Databáze: | OpenAIRE |
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