On the process of cellular division in Escherichia coli: Nucleotide sequence of the gene for penicillin-binding protein 3
| Autor: | Masaaki Soma, Jun-ichi Kato, Masataka Nakamura, Ichiro N. Maruyama, Hideho Suzuki, Yukinori Horota |
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| Rok vydání: | 1983 |
| Předmět: |
DNA
Bacterial Penicillin binding proteins Muramoylpentapeptide Carboxypeptidase Biology medicine.disease_cause Bacterial Proteins Escherichia coli polycyclic compounds Genetics medicine Penicillin-Binding Proteins Coding region Molecular Biology Gene Peptide sequence chemistry.chemical_classification Base Sequence Escherichia coli Proteins Structural gene Nucleic acid sequence biochemical phenomena metabolism and nutrition Molecular biology Amino acid Molecular Weight Genes Hexosyltransferases chemistry Biochemistry Genes Bacterial Peptidyl Transferases bacteria Peptidoglycan Glycosyltransferase Carrier Proteins Cell Division |
| Zdroj: | Molecular and General Genetics MGG. 191:1-9 |
| ISSN: | 1432-1874 0026-8925 |
| DOI: | 10.1007/bf00330881 |
| Popis: | We determined the nucleotide sequence of a DNA fragment containing the ftsI gene coding for the penicillin-binding protein 3 (PBP-3), an indispensable enzyme for cell division of Escherichia coli. The entire ftsI gene was within the 2.8 kilobase PvuII fragment derived from the chromosomal segment on pLC26-6 (Nishimura et al. 1977). The coding region for PBP-3 was identified by comparison with the N-terminal amino acid sequence of in vitro synthesized PBP-3. The structural gene for ftsI consisted of 1,764 base-pairs coding for a 588 amino acid residue-polypeptide with a molecular weight of 63,850. PBP-3 synthesized in vitro showed a lower mobility in SDS-gel electrophoresis than that of the authentic PBP-3, suggesting that the primary translation product of the ftsI gene may be processed to yield mature PBP-3. |
| Databáze: | OpenAIRE |
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