Regulation and secretion of an extracellular esterase from Streptomyces scabies.
Production of a heat-stable, extracellular esterase by Streptomyces scabies is regulated by zinc ions. The esterase-encoding gene (est) from S. scabies was cloned and expressed in Streptomyces lividans. In S. lividans, expression of the est gene is also regulated by Zn2+, and the esterase is efficiently secreted in this organism. The sequence of the est gene suggests that a 39-amino acid signal peptide is removed during secretion of this protein. Deletion analysis has indicated that the hydrophobic domain of the signal peptide is required for secretion. Gel retardation assays and DNaseI footprinting using an S-30 protein extract from S. scabies have previously identified a specific 23-bp protein-binding site upstream from the est coding sequence. Deletion of this protein-binding sequence significantly decreased expression of the est gene.
Schottel
J L
JL
Department of Biochemistry, University of Minnesota, St. Paul 55108.
Hale
V
V
Babcock
M J
MJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000494:pharmacology; D001483:Base Sequence; D004950:Esterases / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D005798:Genes, Bacterial / Q000187:drug effects; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000502:physiology; D013302:Streptomyces / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D015032:Zinc / Q000494:pharmacology
D001426:Bacterial Proteins; D004950:Esterases; D015032:Zinc