@article{mbs:/content/journal/micro/10.1099/00221287-143-3-867, author = "von der Haar, Beate and Walter, Stefan and Schwäpenheer, Susanne and Schrempf, Hildgund", title = "A novel fusidic acid resistance gene from Streptomyces lividans 66 encodes a highly specific esterase", journal= "Microbiology", year = "1997", volume = "143", number = "3", pages = "867-874", doi = "https://doi.org/10.1099/00221287-143-3-867", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-143-3-867", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "Streptomyces lividans 66", keywords = "fusidic-acid-inactivating enzyme", keywords = "FusH gene", keywords = "esterase (FusH)", 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.", }