- Abstract:
-
N(6)-Methyladenosine (m(6)A) is the most prevalent internal RNA modification in eukaryotes. ALKBH5 belongs to the AlkB family of dioxygenases and has been shown to specifically demethylate m(6)A in single-stranded RNA. Here we report crystal structures of ALKBH5 in the presence of either its cofactors or the ALKBH5 inhibitor citrate. Catalytic assays demonstrate that the ALKBH5 catalytic domain can demethylate both single-stranded RNA and single-stranded DNA. We identify the TCA cycle interme...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/jbc.M114.550350
-
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- Journal:
- The Journal of biological chemistry
- Volume:
- 289
- Issue:
- 25
- Pages:
- 17299-17311
- Publication date:
- 2014-06-05
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- URN:
-
uuid:0fd73b62-1f73-42fa-84ab-62b9b9db6e37
- Source identifiers:
-
471093
- Local pid:
- pubs:471093
- Copyright date:
- 2014
Journal article
Structures of human ALKBH5 demethylase reveal a unique binding mode for specific single-stranded N6-methyladenosine RNA demethylation.
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