Deletion of N-terminal End Region of ErmSF Leads to an Amino Acid Having Important Role in Methyl Transfer Reaction

ErmSF에서 특이적으로 발견되는 N-terminal End Region의 점차적인 제거에 의한 활성에 중요한 아미노산의 규명

  • Lee Hak Jin (Department of Genetic Engineering, College of Natural Science, The University of Suwon) ;
  • Jin Hyung Jong (Department of Genetic Engineering, College of Natural Science, The University of Suwon)
  • 이학진 (수원대학교 자연과학대학 생명공학과) ;
  • 진형종 (수원대학교 자연과학대학 생명공학과)
  • Published : 2004.12.01

Abstract

ErmSF is one of the ERM proteins which transfer the methyl group to A2058 in 23S rRNA to confer the resis­tance to MLS (macrolide-lincosamide-streptogramin B) antibiotics on microorganism. Unlike other ERM pro­teins, ErmSF contains long N-terminal end region (NTER), of which $25\%$ is composed of arginine that is known to interact with RNA well. Gradual deletion of NTER leaded us to the point where mutant protein lost much of activity in vivo. Overexpressed and purified mutant protein showed much reduced activity in vitro: $2\%$ activity relative to that of wild type protein. This fact suggests that this amino acid interact with RNA close to meth­ylatable adenine to locate it at an active site properly.

Keywords

ErmSF;in vivo activity;in vivo activity;MLS (macrolide-incosamide-streptogramin B) antibiotic resistance factor protein

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