TY - JOUR
T1 - Characterization of a Streptomyces antibioticus gene cluster encoding a glycosyltransferase involved in oleandomycin inactivation
AU - Hernández, César
AU - Olano, Carlos
AU - Méndez, Carmen
AU - Salas, JoséA A.
N1 - Funding Information:
We wish to thank Eric Cundliffe for providing us the mgt probe. Research in this project was supported by a grant (to J.A.S.) from the Plan National en Biotecnologia (BI091-0758). C.H. was the recipient of a fellowship of S.N.I. and COFAA-IPN (Mexico). C.O. was supported by a grant of the FICYT, Asturias. On request the authors will supply detailed experimental evidence for the conclusions reached in this brief note.
PY - 1993/11/30
Y1 - 1993/11/30
N2 - By homology to the mgt gene (encoding a macrolide glycosyltransferase) from Streptomyces lividans, a 3.3-kb DNA fragment from the oleandomycin producer, Streptomyces antibioticus, was cloned and sequenced. Analysis of the sequence revealed the presence of the 3′ end of a gene (ORF1) and two complete ORFs (ORF2 and oleD), all of them translationally coupled. The deduced product of the sequenced region of ORF1 contained 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 contains 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 product showed clear similarity with several UDP-glucuronosyl- and UDP-glycosyl-transferases from different origins and particularly with the mgt gene from S. lividans, and might encode a glycosyltransferase activity capable of inactivating macrolides. It is proposed that these three genes could participate in the intracellular glycosylation of oleandomycin and its secretion during antibiotic production.
AB - By homology to the mgt gene (encoding a macrolide glycosyltransferase) from Streptomyces lividans, a 3.3-kb DNA fragment from the oleandomycin producer, Streptomyces antibioticus, was cloned and sequenced. Analysis of the sequence revealed the presence of the 3′ end of a gene (ORF1) and two complete ORFs (ORF2 and oleD), all of them translationally coupled. The deduced product of the sequenced region of ORF1 contained 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 contains 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 product showed clear similarity with several UDP-glucuronosyl- and UDP-glycosyl-transferases from different origins and particularly with the mgt gene from S. lividans, and might encode a glycosyltransferase activity capable of inactivating macrolides. It is proposed that these three genes could participate in the intracellular glycosylation of oleandomycin and its secretion during antibiotic production.
KW - Recombinant DNA
KW - antibiotic resistance
KW - macrolides
KW - transport
UR - http://www.scopus.com/inward/record.url?scp=0027385134&partnerID=8YFLogxK
U2 - 10.1016/0378-1119(93)90189-A
DO - 10.1016/0378-1119(93)90189-A
M3 - Artículo
SN - 0378-1119
VL - 134
SP - 139
EP - 140
JO - Gene
JF - Gene
IS - 1
ER -