Primary structure of base non-specific and acid ribonuclease from bullfrog (Rana catesbeiana).

Abstract

A base non-specific acid ribonuclease (RNase RCL2) was purified from bullfrog liver [H. Yagi et al. Biol. Pharm. Bull., 18, 219-222 (1992)]. The sequence study and comparison of the amino acid sequence of the enzyme with homologous RNases from oyster, drosophila and chicken liver suggested that the RNase RCL2 consisted of two components, large protein fraction (182 amino acid residues) and peptide 2 (20 amino acid residues) or peptide 1 (18 amino acid residues), and that both components bind with disulfide bridge. The RNase preparation was probably formed from a single polypeptide protein by processing with some proteases. The amino acid sequence of RNase RCL2 showed that the RNase belongs to the RNase of RNase T2 family and its sequence most resembles chicken liver acid RNase. In RNase RCL2, the amino acid residues which consist of the active site and major base recognition site of RNase Rh, a typical RNase of RNase T2 family, are very well conserved except for Tyr57 (RNase Rh numbering), and part of the amino acid residues of the minor base recognition site (Phe101 and Pro92) are also conserved.