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Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase
Current DNA base editors contain nuclease and DNA deaminase that enables deamination of cytosine (C) or adenine (A), but no method for guanine (G) or thymine (T) editing is available at present. Here we developed a deaminase-free glycosylase-based guanine base editor (gGBE) with G editing ability, b...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10317176/ https://www.ncbi.nlm.nih.gov/pubmed/37404457 http://dx.doi.org/10.1093/nsr/nwad143 |
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author | Tong, Huawei Liu, Nana Wei, Yinghui Zhou, Yingsi Li, Yun Wu, Danni Jin, Ming Cui, Shuna Li, Hengbin Li, Guoling Zhou, Jingxing Yuan, Yuan Zhang, Hainan Shi, Linyu Yao, Xuan Yang, Hui |
author_facet | Tong, Huawei Liu, Nana Wei, Yinghui Zhou, Yingsi Li, Yun Wu, Danni Jin, Ming Cui, Shuna Li, Hengbin Li, Guoling Zhou, Jingxing Yuan, Yuan Zhang, Hainan Shi, Linyu Yao, Xuan Yang, Hui |
author_sort | Tong, Huawei |
collection | PubMed |
description | Current DNA base editors contain nuclease and DNA deaminase that enables deamination of cytosine (C) or adenine (A), but no method for guanine (G) or thymine (T) editing is available at present. Here we developed a deaminase-free glycosylase-based guanine base editor (gGBE) with G editing ability, by fusing Cas9 nickase with engineered N-methylpurine DNA glycosylase protein (MPG). By several rounds of MPG mutagenesis via unbiased and rational screening using an intron-split EGFP reporter, we demonstrated that gGBE with engineered MPG could increase G editing efficiency by more than 1500 fold. Furthermore, this gGBE exhibited high base editing efficiency (up to 81.2%) and high G-to-T or G-to-C (i.e. G-to-Y) conversion ratio (up to 0.95) in both cultured human cells and mouse embryos. Thus, we have provided a proof-of-concept of a new base editing approach by endowing the engineered DNA glycosylase the capability to selectively excise a new type of substrate. |
format | Online Article Text |
id | pubmed-10317176 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-103171762023-07-04 Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase Tong, Huawei Liu, Nana Wei, Yinghui Zhou, Yingsi Li, Yun Wu, Danni Jin, Ming Cui, Shuna Li, Hengbin Li, Guoling Zhou, Jingxing Yuan, Yuan Zhang, Hainan Shi, Linyu Yao, Xuan Yang, Hui Natl Sci Rev Research Article Current DNA base editors contain nuclease and DNA deaminase that enables deamination of cytosine (C) or adenine (A), but no method for guanine (G) or thymine (T) editing is available at present. Here we developed a deaminase-free glycosylase-based guanine base editor (gGBE) with G editing ability, by fusing Cas9 nickase with engineered N-methylpurine DNA glycosylase protein (MPG). By several rounds of MPG mutagenesis via unbiased and rational screening using an intron-split EGFP reporter, we demonstrated that gGBE with engineered MPG could increase G editing efficiency by more than 1500 fold. Furthermore, this gGBE exhibited high base editing efficiency (up to 81.2%) and high G-to-T or G-to-C (i.e. G-to-Y) conversion ratio (up to 0.95) in both cultured human cells and mouse embryos. Thus, we have provided a proof-of-concept of a new base editing approach by endowing the engineered DNA glycosylase the capability to selectively excise a new type of substrate. Oxford University Press 2023-05-16 /pmc/articles/PMC10317176/ /pubmed/37404457 http://dx.doi.org/10.1093/nsr/nwad143 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of China Science Publishing & Media Ltd. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Tong, Huawei Liu, Nana Wei, Yinghui Zhou, Yingsi Li, Yun Wu, Danni Jin, Ming Cui, Shuna Li, Hengbin Li, Guoling Zhou, Jingxing Yuan, Yuan Zhang, Hainan Shi, Linyu Yao, Xuan Yang, Hui Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase |
title | Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase |
title_full | Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase |
title_fullStr | Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase |
title_full_unstemmed | Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase |
title_short | Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase |
title_sort | programmable deaminase-free base editors for g-to-y conversion by engineered glycosylase |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10317176/ https://www.ncbi.nlm.nih.gov/pubmed/37404457 http://dx.doi.org/10.1093/nsr/nwad143 |
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