A bacterial cytidine deaminase toxin enables CRISPR-free mitochondrial base editing

• Published in: Nature (London) Vol. 583; no. 7817; pp. 631 - 637
• Main Authors: Mok, Beverly Y., de Moraes, Marcos H., Zeng, Jun, Bosch, Dustin E., Kotrys, Anna V., Raguram, Aditya, Hsu, FoSheng, Radey, Matthew C., Peterson, S. Brook, Mootha, Vamsi K., Mougous, Joseph D., Liu, David R.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 23.07.2020; Nature Publishing Group
• Subjects: 45/41; 45/70; 631/1647/1511; 631/326/1320; 631/61/201/2110; 631/80/642/333; Bacterial toxins; Bacterial Toxins - chemistry; Bacterial Toxins - genetics; Bacterial Toxins - metabolism; Base Sequence; Biocompatibility; Biomedical materials; Burkholderia cenocepacia - enzymology; Burkholderia cenocepacia - genetics; Cell Respiration - genetics; Chemical properties; CRISPR; Crystal structure; Cytidine - metabolism; Cytidine deaminase; Cytidine Deaminase - chemistry; Cytidine Deaminase - genetics; Cytidine Deaminase - metabolism; Cytosine; Deamination; Deoxyribonucleic acid; DNA; DNA, Mitochondrial - genetics; DNA-binding protein; E coli; Enzymes; Gene Editing - methods; Genes, Mitochondrial - genetics; Genetic aspects; Genetic modification; Genome editing; Genome, Mitochondrial - genetics; Genomes; HEK293 Cells; Humanities and Social Sciences; Humans; Methods; Microbial enzymes; Mitochondria; Mitochondria - genetics; Mitochondrial Diseases - genetics; Mitochondrial Diseases - therapy; Mitochondrial DNA; multidisciplinary; Mutation; Nuclease; Oxidative Phosphorylation; Phosphorylation; Protein Engineering; Proteins; Ribonucleic acid; RNA; RNA, Guide, CRISPR-Cas Systems - genetics; Science; Science (multidisciplinary); Substrate Specificity; Therapeutic applications; Toxins; Transcription; Type VI Secretion Systems - metabolism; Unwinding; Uracil; United States

Bacterial toxins represent a vast reservoir of biochemical diversity that can be repurposed for biomedical applications. Such proteins include a group of predicted interbacterial toxins of the deaminase superfamily, members of which have found application in gene-editing techniques 1 , 2 . Because p...