TAILIEUCHUNG - Báo cáo khoa học: Two overlapping antiparallel genes encoding the iron regulator DmdR1 and the Adm proteins control sidephore and antibiotic biosynthesis in Streptomyces coelicolor A3(2)

ThedmdR1gene ofStreptomyces coelicolorencodes an important regulator of iron metabolism. An antiparallel gene (adm) homologous to a develop-ment-regulated gene ofStreptomyces aureofacienshas been found to over-lap with dmdR1. Both proteins DmdR1 and Adm are formed in solid and liquid cultures of S. coelicolorA3(2). | Two overlapping antiparallel genes encoding the iron regulator DmdRI and the Adm proteins control sidephore and antibiotic biosynthesis in Streptomyces coelicolor A3 2 Sedef Tunca1 Carlos Barreiro1 Juan-Jose R. Coque1 2 and Juan F. Martin1 2 1 Institute of Biotechnology of Leon INBIOTEC Parque Cientifico de Leon Avenida Realno. 1 Spain 2 Area of Microbiology Faculty of Environmentaland BiologicalSciences University of Leon Spain Keywords antibiotics desferrioxamines iron regulation siderophores Streptomyces Correspondence J. F. Martin Instituto de Biotecnologia INBIOTEC Parque Cientifico de Leon Avenida Realno. 1 24006 Leon Spain Fax 34 987 210 388 Tel 34 987 210 308 E-mail Present address Biology Department Faculty of Science Gebze Institute of Technology Kocaeli Turkey Received 13 March 2009 revised 26 May 2009 accepted 29 June 2009 doi The dmdRl gene of Streptomyces coelicolor encodes an important regulator of iron metabolism. An antiparallel gene adm homologous to a development-regulated gene of Streptomyces aureofaciens has been found to overlap with dmdRl. Both proteins DmdR1 and Adm are formed in solid and liquid cultures of S. coelicolor A3 2 . The purpose of this study was to assess possible interaction between the products of these two antiparallel genes. Two mutants with stop codons resulting in arrested translation of either DmdR1 or Adm were obtained by gene replacement and compared with a deletion mutant DdmdRl adm that was defective in both genes. The deletion mutant was unable to form either protein did not sporulate and lacked desferrioxamine actinorhodin and undecylprodigiosin biosynthesis biosynthesis of these compounds was recovered by complementation with dmdRl adm genes. The mutant in which formation of Adm protein was arrested showed normal levels of DmdR1 lacked Adm and overproduced the antibiotics undecylprodigiosin and actinorhodin in MS medium suggesting that Adm plays an important .

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