Characterization of the promoter, signal sequence, and amino terminus of a secreted beta-galactosidase from "Streptomyces lividans".
AUTOR(ES)
Eckhardt, T
RESUMO
The gene for a secreted 130-kilodalton beta-galactosidase from "Streptomyces lividans" has been cloned, its promoter, signal sequence, and amino terminal region have been localized, and their nucleotide sequence has been determined. The signal sequence extends over 56 amino acids and shows the characteristic-features of signal sequences, including a hydrophilic amino terminus followed by a hydrophobic core near the signal cleavage site. The secretion of beta-galactosidase depends on the presence of the signal sequence. beta-Galactosidase is the major protein in culture supernatants and extracts of strains expressing the cloned beta-galactosidase gene and represents a valuable tool in the study of protein secretion in Streptomyces spp.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=213737Documentos Relacionados
- The amino acid sequence of beta-galactosidase of Escherichia coli.
- Cloning and expression of Mycobacterium bovis BCG DNA in "Streptomyces lividans".
- Nucleotide sequence of a thermostable beta-galactosidase from Sulfolobus solfataricus.
- Purification and characterization of a thermotolerant beta-galactosidase from Thermomyces lanuginosus.
- Nucleotide sequence of afsB, a pleiotropic gene involved in secondary metabolism in Streptomyces coelicolor A3(2) and "Streptomyces lividans".
