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Biochemical characterization of RNase R 2'-O-methylation sensitivity.
Lu, Xiaolan; Gu, Xiangwen; Li, Yong; Wu, Yifan; Wang, Qiang; Yu, Wenkui; Chen, Qihan.
Afiliación
  • Lu X; Nanjing Drum Tower Hospital, The Affiliated Hospital of Nanjing University Medical School, Nanjing, Jiangsu, 210093, China; Medical School of Nanjing University, Nanjing, Jiangsu, 210093, China.
  • Gu X; The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, Jiangsu, 210023, China.
  • Li Y; The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, Jiangsu, 210023, China.
  • Wu Y; The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, Jiangsu, 210023, China.
  • Wang Q; The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, Jiangsu, 210023, China.
  • Yu W; Nanjing Drum Tower Hospital, The Affiliated Hospital of Nanjing University Medical School, Nanjing, Jiangsu, 210093, China.
  • Chen Q; Medical School of Nanjing University, Nanjing, Jiangsu, 210093, China. Electronic address: chenqihan@nju.edu.cn.
Biochimie ; 212: 106-113, 2023 Sep.
Article en En | MEDLINE | ID: mdl-37105299
RNase R is a member of the RNA exonuclease family that digests RNA in the 3'-5' direction. Previous studies have identified RNase R from Mycoplasma genitalium (MgR) as the only RNA exonuclease that is sensitive to 2'-O-methylation (Nm) modification. However, the mechanism underlying this characteristic is not well understood. In this study, we aimed to explore the molecular mechanism of RNase R Nm sensitivity using an improved assay that can better evaluate Nm sensitivity. By comparing the sequences of five wild-type RNase R variants from Mycoplasma, we identified the importance of loop 18 in Nm sensitivity. Furthermore, we demonstrated the critical roles of L283, T278, and T279 within loop18. Our findings deepen the understanding of the molecular mechanism of why MgR is sensitive to Nm and provide a potential direction of protein engineering for applications.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Exonucleasas / Exorribonucleasas Tipo de estudio: Diagnostic_studies / Prognostic_studies Idioma: En Revista: Biochimie Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Francia
Texto completo
Añadir a Mi BVS
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Exonucleasas / Exorribonucleasas Tipo de estudio: Diagnostic_studies / Prognostic_studies Idioma: En Revista: Biochimie Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Francia