Structures of a mobile intron retroelement poised to attack its structured DNA target.
Journal
Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511
Informations de publication
Date de publication:
11 11 2022
11 11 2022
Historique:
entrez:
10
11
2022
pubmed:
11
11
2022
medline:
15
11
2022
Statut:
ppublish
Résumé
Group II introns are ribozymes that catalyze their self-excision and function as retroelements that invade DNA. As retrotransposons, group II introns form ribonucleoprotein (RNP) complexes that roam the genome, integrating by reversal of forward splicing. Here we show that retrotransposition is achieved by a tertiary complex between a structurally elaborate ribozyme, its protein mobility factor, and a structured DNA substrate. We solved cryo-electron microscopy structures of an intact group IIC intron-maturase retroelement that was poised for integration into a DNA stem-loop motif. By visualizing the RNP before and after DNA targeting, we show that it is primed for attack and fits perfectly with its DNA target. This study reveals design principles of a prototypical retroelement and reinforces the hypothesis that group II introns are ancient elements of genetic diversification.
Identifiants
pubmed: 36356138
doi: 10.1126/science.abq2844
pmc: PMC10190682
mid: NIHMS1870836
doi:
Substances chimiques
Retroelements
0
Ribonucleoproteins
0
RNA, Catalytic
0
RNA-Directed DNA Polymerase
EC 2.7.7.49
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
627-634Subventions
Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : NIH HHS
ID : S10 OD023603
Pays : United States
Commentaires et corrections
Type : CommentIn
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