Cargando…
A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets
Mobile group II introns are site-specific retrotransposable elements abundant in bacterial and organellar genomes. They are composed of a large and highly structured ribozyme and an intron-encoded reverse transcriptase that binds tightly to its intron to yield a ribonucleoprotein (RNP) particle. Dur...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8643678/ https://www.ncbi.nlm.nih.gov/pubmed/34791436 http://dx.doi.org/10.1093/nar/gkab1031 |
_version_ | 1784609907630145536 |
---|---|
author | Monachello, Dario Lauraine, Marc Gillot, Sandra Michel, François Costa, Maria |
author_facet | Monachello, Dario Lauraine, Marc Gillot, Sandra Michel, François Costa, Maria |
author_sort | Monachello, Dario |
collection | PubMed |
description | Mobile group II introns are site-specific retrotransposable elements abundant in bacterial and organellar genomes. They are composed of a large and highly structured ribozyme and an intron-encoded reverse transcriptase that binds tightly to its intron to yield a ribonucleoprotein (RNP) particle. During the first stage of the mobility pathway, the intron RNA catalyses its own insertion directly into the DNA target site. Recognition of the proper target rests primarily on multiple base-pairing interactions between the intron RNA and the target DNA, while the protein makes contacts with only a few target positions by yet-unidentified mechanisms. Using a combination of comparative sequence analyses and in vivo mobility assays we demonstrate the existence of a new base-pairing interaction named EBS2a–IBS2a between the intron RNA and its DNA target site. This pairing adopts a Watson–Crick geometry and is essential for intron mobility, most probably by driving unwinding of the DNA duplex. Importantly, formation of EBS2a–IBS2a also requires the reverse transcriptase enzyme which stabilizes the pairing in a non-sequence-specific manner. In addition to bringing to light a new structural device that allows subgroup IIB1 and IIB2 introns to invade their targets with high efficiency and specificity our work has important implications for the biotechnological applications of group II introns in bacterial gene targeting. |
format | Online Article Text |
id | pubmed-8643678 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-86436782021-12-06 A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets Monachello, Dario Lauraine, Marc Gillot, Sandra Michel, François Costa, Maria Nucleic Acids Res Nucleic Acid Enzymes Mobile group II introns are site-specific retrotransposable elements abundant in bacterial and organellar genomes. They are composed of a large and highly structured ribozyme and an intron-encoded reverse transcriptase that binds tightly to its intron to yield a ribonucleoprotein (RNP) particle. During the first stage of the mobility pathway, the intron RNA catalyses its own insertion directly into the DNA target site. Recognition of the proper target rests primarily on multiple base-pairing interactions between the intron RNA and the target DNA, while the protein makes contacts with only a few target positions by yet-unidentified mechanisms. Using a combination of comparative sequence analyses and in vivo mobility assays we demonstrate the existence of a new base-pairing interaction named EBS2a–IBS2a between the intron RNA and its DNA target site. This pairing adopts a Watson–Crick geometry and is essential for intron mobility, most probably by driving unwinding of the DNA duplex. Importantly, formation of EBS2a–IBS2a also requires the reverse transcriptase enzyme which stabilizes the pairing in a non-sequence-specific manner. In addition to bringing to light a new structural device that allows subgroup IIB1 and IIB2 introns to invade their targets with high efficiency and specificity our work has important implications for the biotechnological applications of group II introns in bacterial gene targeting. Oxford University Press 2021-11-17 /pmc/articles/PMC8643678/ /pubmed/34791436 http://dx.doi.org/10.1093/nar/gkab1031 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Nucleic Acid Enzymes Monachello, Dario Lauraine, Marc Gillot, Sandra Michel, François Costa, Maria A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets |
title | A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets |
title_full | A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets |
title_fullStr | A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets |
title_full_unstemmed | A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets |
title_short | A new RNA–DNA interaction required for integration of group II intron retrotransposons into DNA targets |
title_sort | new rna–dna interaction required for integration of group ii intron retrotransposons into dna targets |
topic | Nucleic Acid Enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8643678/ https://www.ncbi.nlm.nih.gov/pubmed/34791436 http://dx.doi.org/10.1093/nar/gkab1031 |
work_keys_str_mv | AT monachellodario anewrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT laurainemarc anewrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT gillotsandra anewrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT michelfrancois anewrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT costamaria anewrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT monachellodario newrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT laurainemarc newrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT gillotsandra newrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT michelfrancois newrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets AT costamaria newrnadnainteractionrequiredforintegrationofgroupiiintronretrotransposonsintodnatargets |