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Keywords
- RNA (7)
- in vitro selection (6)
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- deoxyribozymes (3)
- Chili RNA Aptamer (2)
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- N6-methyladenosine (m6A) (1)
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- RNA Aptamer (1)
- RNA Labelling (1)
- RNA Methyltransferase (1)
- RNA Modification (1)
- RNA aptamers (1)
- RNA cleavage (1)
- RNA labeling (1)
- RNA ligation (1)
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- YTH reader proteins (1)
- alkene-alkyne [2+2] photocycloaddition (1)
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- artificial base pair (1)
- atomic mutagenesis (1)
- bioorthogonal SAM analogue ProSeDMA (1)
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- demethylase enzymes FTO and ALKBH5 (1)
- dipole-dipole interaction (1)
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- stokes shift (1)
- structural biology (1)
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- structure probing (1)
- tenofovir (1)
- trans-acting 2'-5' adenylyl transferase ribozymes (1)
Institute
Schriftenreihe
Sonstige beteiligte Institutionen
- International Max Planck Research School Molecular Biology, University of Göttingen, Germany (2)
- Agricultural Center, BASF SE, 67117 Limburgerhof, Germany (1)
- Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), Göttingen, Germany (1)
- Center for Nanosystems Chemistry (CNC), University of Würzburg (1)
- Cluster of Excellence "Multiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells, Göttingen (1)
- Department of Cellular Biochemistry, University Medical Center Göttingen (1)
- Department of Cellular Biochemistry, University Medical Centre Göttingen (1)
- Department of Molecular Biology, University Medical Center Göttingen, Germany (1)
- Department of Molecular Biology, University Medical Centre Göttingen (1)
- Department of Molecular Biology, University Medical Centre Göttingen, Göttingen 37073, Germany (1)
N\(^6\)-methyladenosine (m\(^6\)A) is an important modified nucleoside in cellular RNA associated with multiple cellular processes and is implicated in diseases. The enzymes associated with the dynamic installation and removal of m\(^6\)A are heavily investigated targets for drug research, which requires detailed knowledge of the recognition modes of m\(^6\)A by proteins. Here, we use atomic mutagenesis of m\(^6\)A to systematically investigate the mechanisms of the two human m\(^6\)A demethylase enzymes FTO and ALKBH5 and the binding modes of YTH reader proteins YTHDF2/DC1/DC2. Atomic mutagenesis refers to atom-specific changes that are introduced by chemical synthesis, such as the replacement of nitrogen by carbon atoms. Synthetic RNA oligonucleotides containing site-specifically incorporated 1-deaza-, 3-deaza-, and 7-deaza-m\(^6\)A nucleosides were prepared by solid-phase synthesis and their RNA binding and demethylation by recombinant proteins were evaluated. We found distinct differences in substrate recognition and transformation and revealed structural preferences for the enzymatic activity. The deaza m\(^6\)A analogues introduced in this work will be useful probes for other proteins in m\(^6\)A research.