DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs.
Animals
Coenzyme A
/ metabolism
Exoribonucleases
/ chemistry
Flavin-Adenine Dinucleotide
/ analysis
HEK293 Cells
Humans
In Vitro Techniques
Kluyveromyces
/ enzymology
Mice
Models, Molecular
NAD
/ metabolism
Nuclear Proteins
/ chemistry
RNA Caps
/ analysis
RNA, Messenger
/ chemistry
Schizosaccharomyces pombe Proteins
/ metabolism
Substrate Specificity
Transcription, Genetic
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
19 06 2020
19 06 2020
Historique:
accepted:
16
04
2020
revised:
14
04
2020
received:
26
02
2020
pubmed:
7
5
2020
medline:
9
9
2020
entrez:
7
5
2020
Statut:
ppublish
Résumé
In eukaryotes, the DXO/Rai1 enzymes can eliminate most of the incomplete and non-canonical NAD caps through their decapping, deNADding and pyrophosphohydrolase activities. Here, we report that these enzymes can also remove FAD and dephospho-CoA (dpCoA) non-canonical caps from RNA, and we have named these activities deFADding and deCoAping. The crystal structures of mammalian DXO with 3'-FADP or CoA and fission yeast Rai1 with 3'-FADP provide elegant insight to these activities. FAD and CoA are accommodated in the DXO/Rai1 active site by adopting folded conformations. The flavin of FAD and the pantetheine group of CoA contact the same region at the bottom of the active site tunnel, which undergoes conformational changes to accommodate the different cap moieties. We have developed FAD-capQ to detect and quantify FAD-capped RNAs and determined that FAD caps are present on short RNAs (with less than ∼200 nucleotides) in human cells and that these RNAs are stabilized in the absence of DXO.
Identifiants
pubmed: 32374864
pii: 5831185
doi: 10.1093/nar/gkaa297
pmc: PMC7293010
doi:
Substances chimiques
Nuclear Proteins
0
RNA Caps
0
RNA, Messenger
0
Schizosaccharomyces pombe Proteins
0
NAD
0U46U6E8UK
Flavin-Adenine Dinucleotide
146-14-5
dephosphocoenzyme A
3633-59-8
Dxo protein, mouse
EC 3.1.-
Exoribonucleases
EC 3.1.-
Rai1 protein, S pombe
EC 3.1.-
Coenzyme A
SAA04E81UX
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
6136-6148Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM067005
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM118093
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103403
Pays : United States
Organisme : NIH HHS
ID : S10 OD012018
Pays : United States
Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
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