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KMID : 0364820140500030239
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Korean Journal of Microbiology
2014 Volume.50 No. 3 p.239 ~ p.244
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Effect of Truncation of 38 Amino Acids in N-terminal Region of ErmSF,a MLSB Antibiotic Resistance Factor Protein, on Enzymatic Activity
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Lee Hak-Jin
Jin Hyung-Jong
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Abstract
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ErmSF is one of the four antibiotic resistance factor proteins expressed by Streptomyces fradiae, antibiotic tylosin
producer, which renders MLSB (macrolide-lincosamide-streptogramin B) antibiotic resistance through dimethylating
A2058 of 23S rRNA, thereby reducing the affinity of antibiotic to ribosome. Unlike other Erm proteins, ErmSF
harbors long N-terminal end region. To investigate its role in enzyme activity, mutant ErmSF deleted of 1?38 amino
acids was overexpressed and activity in vivo and in vitro was observed. In vitro enzymatic assay showed that mutant
protein exhibited reduced activity by 20% compared to the wild type enzyme. Due to the reduced activity of the
mutant protein, cells expressing mutant protein showed weaker resistance to erythromycin than cells with wild type
enzyme. Presumably, the decrease in enzyme activity was caused by the hindrance in substrate binding and (or)
product release, not by defect in the methyl group transfer occurred in active site.
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KEYWORD
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23S rRNA methylation, antibiotic resistance, deletion mutation of protein, ErmSF, in vivo and in vitro enzyme activity, MLSB antibiotic resistance factor protein, N-terminal end region
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