In:
Journal of Bacteriology, American Society for Microbiology, Vol. 169, No. 6 ( 1987-06), p. 2691-2696
Abstract:
A gene bank was constructed from Pseudomonas aeruginosa PAO1 and used to complement three P. aeruginosa elastase-deficient strains. One clone, pRF1, contained a gene which restored elastase production in two P. aeruginosa isolates deficient in elastase production (PA-E15 and PAO-E105). This gene also encoded production of elastase antigen and activity in Escherichia coli and is the structural gene for Pseudomonas elastase. A second clone, pHN13, contained a 20-kilobase (kb) EcoRI insert which was not related to the 8-kb EcoRI insert of pRF1 as determined by restriction analysis and DNA hybridization. A 2.2-kb SalI-HindIII fragment from pHN3 was subcloned into pUC18, forming pRB1822-1. Plasmid pRB1822-1 restored normal elastolytic activity to PAO-E64, a mutant for elastase activity. Clones derived from pHN13 failed to elicit elastase antigen or enzymatic activity in E. coli.
Type of Medium:
Online Resource
ISSN:
0021-9193
,
1098-5530
DOI:
10.1128/jb.169.6.2691-2696.1987
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
1987
detail.hit.zdb_id:
1481988-0
SSG:
12