The RRM of the kRNA-editing protein TbRGG2 uses multiple surfaces to bind and remodel RNA.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
28 02 2019
28 02 2019
Historique:
accepted:
11
12
2018
revised:
29
11
2018
received:
03
10
2018
pubmed:
14
12
2018
medline:
28
8
2019
entrez:
14
12
2018
Statut:
ppublish
Résumé
Kinetoplastid RNA (kRNA) editing takes place in the mitochondria of kinetoplastid protists and creates translatable mRNAs by uridine insertion/deletion. Extensively edited (pan-edited) transcripts contain quadruplex forming guanine stretches, which must be remodeled to promote uridine insertion/deletion. Here we show that the RRM domain of the essential kRNA-editing factor TbRGG2 binds poly(G) and poly(U) RNA and can unfold both. A region C-terminal to the RRM mediates TbRGG2 dimerization, enhancing RNA binding. A RRM-U4 RNA structure reveals a unique RNA-binding mechanism in which the two RRMs of the dimer employ aromatic residues outside the canonical RRM RNA-binding motifs to encase and wrench open the RNA, while backbone atoms specify the uridine bases. Notably, poly(G) RNA is bound via a different binding surface. Thus, these data indicate that TbRGG2 RRM can bind and remodel several RNA substrates suggesting how it might play multiple roles in the kRNA editing process.
Identifiants
pubmed: 30544166
pii: 5245446
doi: 10.1093/nar/gky1259
pmc: PMC6393287
doi:
Substances chimiques
RNA, Protozoan
0
RNA
63231-63-0
Uridine
WHI7HQ7H85
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
2130-2142Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM130290
Pays : United States
Informations de copyright
© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.
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