Isolation of acetyl esterase mutants of Bacillus subtilis 168.
AUTOR(ES)
Higerd, T B
RESUMO
Five mutants of Bacillus subtilis 168 defective in an intracellular esterase activity were identified. By polyacrylamide gel electrophoresis, four of the mutants were shown to lack esterase B activity, and the fifth lacked esterase A activity. All of the back-crossed esterase mutants were able to sporulate at wild-type frequency and produce exoprotease(s) and antibiotic(s). No difference in motility could be attributed to the esterase mutation. PBS1 transduction analysis showed all the esterase B mutations to be linked to the hisA marker.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=235036Documentos Relacionados
- Autolytic enzyme-deficient mutants of Bacillus subtilis 168.
- Bidirectional chromosome replication in Bacillus subtilis 168.
- Aspartokinase III, a new isozyme in Bacillus subtilis 168.
- Isolation, characterization, and mapping of Bacillus subtilis 168 germination mutants.
- Control of chromosome replication in thymine-requiring strains of Bacillus subtilis 168.
