Phosphorothioate (PT)-modification was discovered in prokaryotes and is involved in many
biological functions such as restriction-modification systems. PT-modification can be …

DNA phosphorothioate (PT)-modification, with a non-bridging oxygen in the phosphodiester
backbone substituted by sulfur, is an epigenetic marker in prokaryotes and involved in the …

Site-directed RNA editing is an important technique for correcting gene sequences and
ultimately tuning protein function. In this study, we engineered the deaminase domain of …

The sulfur atom of phosphorothioated DNA (PT-DNA) is coordinated by a surface cavity in
the conserved sulfur-binding domain (SBD) of type IV restriction enzymes. However, some …

Site-directed RNA base editing enables the transient and dosable change of genetic
information and represents a recent strategy to manipulate cellular processes, paving ways …

Synthetic phosphorothioate (PT) internucleotide linkages, in which a nonbridging oxygen is
replaced by a sulphur atom, share similar physical and chemical properties with …

Bacterial DNA phosphorothioate (PT) modification provides a specific anchoring site for
sulfur-binding proteins (SBDs). Besides, their recognition patterns include phosphate links …

Selective genome editing such as gene knock-in has recently been achieved by
administration of chemical enhancer or inhibitor of particular DNA double-strand break …

Highlights•RNA editing is an attractive, complementing alternative to gene editing.•Several
RNA-guided editases have been engineered all suffering from off-targets.•dCas13-based …

There have been very few reports on protein domains that specifically recognize sulfur. Here
we present the crystal structure of the sulfur-binding domain (SBD) from the DNA …