Volume 8, Issue 3, Pages (March 2001)

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Volume 8, Issue 3, Pages 253-263 (March 2001) Identification of a sugar flexible glycosyltransferase from Streptomyces olivaceus, the producer of the antitumor polyketide elloramycin  Gloria Blanco, Eugenio P Patallo, Alfredo F Braña, Axel Trefzer, Andreas Bechthold, Jürgen Rohr, Carmen Méndez, José A Salas  Chemistry & Biology  Volume 8, Issue 3, Pages 253-263 (March 2001) DOI: 10.1016/S1074-5521(01)00010-2

Fig. 1 (A) Structures of elloramycin, 8-DMTC and mithramycin. (B) Schematic representation of the restriction map of cosmid 16F4: the shadowed bar indicates the region that has been shown to hybridize with the tcmAGNPKLM genes of the tetracenomycin C gene cluster [17]. The black bar shows the location of the fragment hybridizing against the 350 bp PCR probe. The black triangle represents the ermEp. B, BamHI; M, MboI; P, PstI; S, SalI. Chemistry & Biology 2001 8, 253-263DOI: (10.1016/S1074-5521(01)00010-2)

Fig. 2 Nucleotide sequence of the 1850 bp DNA region sequenced containing elmGT. The complete nucleotide sequence of the fragment is shown with the deduced amino acid sequence of elmGT in a single letter code. The sequence has been deposited in GenBank under the accession number AJ300305. Chemistry & Biology 2001 8, 253-263DOI: (10.1016/S1074-5521(01)00010-2)

Fig. 2 Nucleotide sequence of the 1850 bp DNA region sequenced containing elmGT. The complete nucleotide sequence of the fragment is shown with the deduced amino acid sequence of elmGT in a single letter code. The sequence has been deposited in GenBank under the accession number AJ300305. Chemistry & Biology 2001 8, 253-263DOI: (10.1016/S1074-5521(01)00010-2)

Fig. 3 (A) Alignment of the deduced amino acid sequences of different glycosyltransferases around the conserved regions chosen for designing the two oligoprimers for PCR amplification. FP and RP indicate the amino acid regions selected for the forward and reverse primer, respectively. IroB, glycosyltransferase from S. typhi[24]; SnogD, glycosyltransferase from S. nogalater[23]; UrdGT1b and UrdGT1c, glycosyltransferases from S. fradiae[3]; OleG2, glycosyltransferase from S. antibioticus[8]; LanGT2, glycosyltransferase from S. cyanogenus[11]; MtmGII, glycosyltransferase from S. argillaceus[7]. (B) Dendrogram showing the similarities among different glycosyltransferases: all glycosyltransferases shown are involved in antibiotic biosynthesis in producer organisms, with the exception of IroB. Chemistry & Biology 2001 8, 253-263DOI: (10.1016/S1074-5521(01)00010-2)

Fig. 4 Structures of 8-DMTC and 6-DOH (substituted at R) forming part of novel glycosylated tetracenomycin derivatives generated with the participation of the ElmGT glycosyltransferase. Chemistry & Biology 2001 8, 253-263DOI: (10.1016/S1074-5521(01)00010-2)

Chemistry & Biology 2001 8, 253-263DOI: (10 Chemistry & Biology 2001 8, 253-263DOI: (10.1016/S1074-5521(01)00010-2)