• Microbiology and Biotechnology Letters
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• v.19 no.3
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• pp.235-241
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• 1991

- A phthalic acid derivative and basic macrolide antibiotics, with antimicrobial activity against Gram positive bacteria and phytopathogenic fungi, respectively, were found to be produced by a strain 88-GT-161 identified as being a variety of Streptomyces melanosporofaciens. This paper describes an isolation procedure of the active compounds produced by this strain, their in vitro and in vivo (pot test) antimicrobial activites, and structure determination of one of the compounds, bis (2-ethylhexyl) phthalate, a phthalic acid derivative antibiotic. This compounds, upon cornparision with authentic bis (2-ethylhexyl) phthalate, dioctyl phthalate, revealed a difference in antimicrobial activity even though physico-chemical properties of these two compounds seemed indentical. This is the first report that dioctyl phthalate is biosynthetically produced by a Streptomyces sp. and shows antimicrobial activity.

• Microbiology and Biotechnology Letters
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• v.18 no.6
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• pp.624-632
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• 1990

Strain 88-GT-161 producing new phthalic acid derivative and basic macrolide antibiotics was identified as being S. melanosporofuciens based on numerical taxonomic data. However, 4 unit characters among 139 units were clearly different from the common properties of 6 strains belonging to cluster No. 32 represented by the name of S. violaceoniger or S. violaceusniger, leading us to designate as a variety of S. melunosporofaciens. This paper describes the taxonomic characteristics of the strain. Isolation and chemical structures, including biological activities of the active compounds produced by this strain will be presented elsewhere.

• Korean Journal of Microbiology
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• v.48 no.2
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• pp.79-86
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• 2012

ErmSF is one of the Erm family proteins which catalyze S-adenosyl-$_L$-methionine dependent modification of a specific adenine residue (A2058, E. coli numbering) in bacterial 23S rRNA, thereby conferring resistance to clinically important macrolide, lincosamide and streptogramin B ($MLS_B$) antibiotics. $^{222}FXPXPXVXS^{230}$ (ErmSF numbering) sequence appears to be a consensus sequence among the Erm family. This sequence was supposed to be involved in direct interaction with the target adenine from the structural studies of Erm protein ErmC'. But in DNA methyltarnsferase M. Taq I, this interaction have been identified biochemically and from the complex structure with substrate. Arginine 223 and 227 in this sequence are not conserved among Erm proteins, but because of the basic nature of residues, it was expected to interact with RNA substrates. Two amino acid residues were replaced with Ala by site-directed mutagenesis. Two mutant proteins still maintained its activity in vivo and resistant to the antibiotic erythromycin. Compared to the wild-type ErmSF, R223A and R227A proteins retained about 50% and 88% of activity in vitro, respectively. Even though those arginine residues are not essential in the catalytic step, with their positive charge they may play an important role for RNA binding.