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Preparation of Human Nuclear RNA m6A Methyltransferases and Demethylases and Biochemical Characterization of Their Catalytic Activity.
Liu, Jianzhao; Yue, Yanan; He, Chuan.
Afiliación
  • Liu J; Department of Chemistry, The University of Chicago, Chicago, Illinois, USA; Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois, USA; Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois, USA.
  • Yue Y; Department of Chemistry, The University of Chicago, Chicago, Illinois, USA; Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois, USA; Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois, USA.
  • He C; Department of Chemistry, The University of Chicago, Chicago, Illinois, USA; Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois, USA; Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois, USA; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA. Electronic address: chuanhe@uchicago.edu.
Methods Enzymol ; 560: 117-30, 2015.
Article en En | MEDLINE | ID: mdl-26253968
N(6)-Methyladenosine (m(6)A) represents the most prevalent internal modification in messenger and long noncoding RNAs. There has been a surge of interest toward understanding the biological significance of m(6)A modification. In this chapter, we describe the methods for biochemically studying the recently uncovered m(6)A methyltransferases (METTL3 and METTL14) and demethylases (FTO and ALKBH5). How to express these proteins, perform their biochemistry reactions against various RNA probes, and characterize the methylation and demethylation activity will be discussed.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: ARN Nuclear / Adenosina / ARN Largo no Codificante Límite: Humans Idioma: En Revista: Methods Enzymol Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: ARN Nuclear / Adenosina / ARN Largo no Codificante Límite: Humans Idioma: En Revista: Methods Enzymol Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos