The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures
- 1 March 1990
- journal article
- research article
- Published by Wiley in Molecular Microbiology
- Vol. 4 (3) , 513-517
- https://doi.org/10.1111/j.1365-2958.1990.tb00618.x
Abstract
Comparison of the predicted amino acid sequence of the cell-cycle RodA protein with the National Research Foundation protein sequence database shows that the 370-amino-acid RodA, a protein that is essential for wall elongation in Escherichia coli and maintenance of the rod shape of the cell, is highly analogous, in terms of primary structure, with the Bacillus subtilis SpoVE protein involved in stage V of sporulation.Keywords
This publication has 55 references indexed in Scilit:
- Membrane topology of penicillin‐binding protein 3 of Escherichia coliMolecular Microbiology, 1989
- Overexpression, solubilization and refolding of a genetically engineered derivative of the penicillin‐binding protein 3 of Escherichia coli K12Molecular Microbiology, 1988
- A water-soluble form of penicillin-binding protein 2 ofEscherichia coliconstructed by site-directed mutagenesisFEBS Letters, 1987
- Prokaryotic and eukaryotic cell-cycle proteinsNature, 1987
- Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin‐binding protein 2 of Escherichia coli K12European Journal of Biochemistry, 1986
- Overproduction of FtsZ induces minicell formation in E. coliCell, 1985
- The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coliGene, 1985
- Differential expression of penicillin-binding protein structural genes during Bacillus subtilis sporulationFEMS Microbiology Letters, 1983
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Sporulation in Bacillus subtilis. Characterization of Oligosporogenous Mutants and Comparison of Their Phenotypes with Those of Asporogenous MutantsJournal of General Microbiology, 1972