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A novel fusidic acid resistance gene from Streptomyces lividans 66 encodes a highly specific esterase

Universität Osnabrück, FB Biologie/Chemie, Barbarastraße 11, 49069 Osnabrück, Germany

ABSTRACT

Resistance to fusidic acid in Streptomyces lividans is due to secretion of an extracellular enzyme (FusH) that converts the steroid antibiotic into an inactive derivative. NH₂-terminal and several internal amino acid sequences were prepared from the purified enzyme. Using one of the deduced oligonucleotides to probe a subgenomic DNA library, the fusH gene was cloned and sequenced. Sequence analysis located an ORF which, owing to the presence of two putative start codons, indicates a predicted protein with 520 or 509 amino acids. A signal peptide was identified by aligning the deduced amino acids with the N-terminal sequence determined for the mature enzyme. The C-terminal part of the deduced FusH contains a region of three tandemly repeated stretches of 50 amino acids, which is preceded and followed by amino acids showing high homology with the repeats. FusH was found to share a GDS motif with some deduced esterases. S. lividans transformants carrying fusH on a multicopy vector synthesized high levels of FusH. Purified FusH cleaved equally well an acetyl, a thioacetyl or a formyl group from the 16β-position of fusidic acid and its derivatives. However, a propionyl group at the 16β-position was attacked with difficulty and a 16β-acetyl group was not hydrolysed at all. These data indicate that FusH is a highly specific esterase. The fusH gene is widely distributed among streptomycetes that modify fusidic acid to its inactive lactone derivative.

^*Author for correspondence: Hildgund Schrempf. Tel: +49 541 969 2895. Fax: +49 541 969 2804. e-mail: schrempf@sfbbiol.biologie.uni-osnabrueck.de

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