C. Hernandez et al., CHARACTERIZATION OF A STREPTOMYCES-ANTIBIOTICUS GENE-CLUSTER ENCODINGA GLYCOSYLTRANSFERASE INVOLVED IN OLEANDOMYCIN INACTIVATION, Gene, 134(1), 1993, pp. 139-140
By homology to the mgt gene (encoding a macrolide glycosyltransferase)
from Streptomyces lividans, a 3.3-kb DNA fragment from the oleandomyc
in producer, Streptomyces antibioticus, was cloned and sequenced. Anal
ysis of the sequence revealed the presence of the 3' end of a gene (OR
F1) and two complete ORFs (ORF2 and oleD), ali of them translationally
coupled. The deduced product of the sequenced region of ORF1 containe
d the typical signature of integral membrane proteins responsible for
the translocation of substrates across the membrane. The ORF2 product
did not show significant similarity with proteins in databases, but co
ntains an N-terminus leader peptide region characteristic of secreted
proteins, and a lipid attachment site motif characteristic of membrane
lipoproteins synthesized with a precursor signal peptide. The oleD pr
oduct showed clear similarity with several UDP-glucuronosyl- and UDP-g
lycosyl-transferases from different origins and particularly with the
mgt gene from S. lividans, and might encode a glycosyltransferase acti
vity capable of inactivating macrolides. It is proposed that these thr
ee genes could participate in the intracellular glycosylation of olean
domycin and its secretion during antibiotic production.