Abstract: It was found that four nuclease domain mutants have nuclease activity superior to that of a wild-type nuclease domain and are capable of enhancing genome editing efficiency in combination with various nucleic acid binding domains.

Abstract: A method for converting an editing target C contained in a target RNA to U or an editing target U contained in a target RNA to C is provided. A method for editing a target RNA, which comprises applying an artificial DYW protein containing a DYW domain consisting of any one of the polypeptides a, b, c, and be mentioned below to the target RNA: a. a polypeptide having xa1PGxa1SWIExa3-xa16HP . . . HxaaE . . . Cxa17Xa18CH . . . DYW, having a sequence identity of at least 40% to the sequence of SEQ ID NO: 1, and having a C-to-U/U-to-C editing activity, b. a polypeptide having xb1PGxb2SWWTDxb3-xb16HP . . . HxbbE . . . Cxb17xb18CH . . . DYW, having a sequence identity of at least 40% to the sequence of SEQ ID NO: 2, and having a C-to-U/U-to-C editing activity, c. a polypeptide having KPAxc1Axc2IExc3 . . . HxccE . . . Cxc4xc5CH . . . xc6xc7xc8, having a sequence identity of at least 40% to the sequence of SEQ ID NO: 3, and having a C-to-U/U-to-C editing activity, and be. a polypeptide having xb1PGxb2SWWTDxb3-xb16HP .

Abstract: A PPR protein with high performance is provided. A PPR protein that binds to a long nucleotide sequence is provided by linking motifs in a number larger than conventionally used 7 to 14. A PPR motif is provided, of which typical examples are the followings: (A-1) a PPR motif consisting of the sequence of SEQ ID NO: 9 or 401, (C-1) a PPR motif consisting of the sequence of SEQ ID NO: 10, (G-1) a PPR motif consisting of the sequence of SEQ ID NO: 11, and (U-1) a PPR motif consisting of the sequence of SEQ ID NO: 12. These motifs are useful as PPR motifs for adenine, cytosine, guanine, and uracil in a target nucleotide sequence, respectively.

Abstract: In order to improve aggregation property of a PPR protein, the A6 amino acid of the 1st PPR motif from the N-terminus (M1) is made more hydrophilic. Further, the A9 amino acid of M1 is made to be a hydrophilic amino acid or glycine. The A6 amino acid is preferably asparagine or aspartic acid, and the A9 amino acid is preferably glutamine, glutamic acid, lysine, or glycine. Proteins containing such a PPR motif as M1 motif may have not only improved aggregation property, but also high binding power to a target nucleic acid.