Base Specificity and Primary Structure of Poly U-preferential Ribonuclease from Chicken Liver

Abstract

The primary structure and base specificity of chicken liver RNase CL1 which has been reported by Miura et al. [Chem. Pharm. Bull., 32, 4053-4060 (1984)] as poly U-preferential RNase, were extensively studied. The sequence study of this enzyme and comparison of the amino acid sequence of the enzyme with homologous RNases from oyster and Drosophila melanogaster suggested that RNase CL1 consists of three peptides with 17, 19, and 163 amino acid residues. The amino acid sequence of these three peptides were identified. The two small peptides are joined to the large peptide by disulfide bridges. The amino acid sequence of RNase CL1 had 62 (31.2%) and 63 residues (31.6%) identical with oyster RNase and D. melanogaster RNase, respectively, and belongs to the RNase T2 family RNase. Reassessment of the base specificity of RNase CL1 found that it is guanylic acid, then uridylic acid-preferential, and not poly U preferential.

Primary Structure and Properties of Ribonuclease Bm2 (RNase Bm2) from Bryopsis maxima

“…In RNase Bm2, D51, Y57, and W49 at the B1 site of RNase Rh were replaced by Asn (N50 in RNase Bm2), Trp (W56), and ; Rh, RNase Rh from Rhizopus niveus 19) ; RNase T2 from Aspergillus oryzae 20) ; RNase Le2 from Lentinus edodes 21) ; RNase Phyb from Physarum polycepharum 22) ; RNase Dd1 from Dictiostelium discoidium 23) ; Bm2, RNase Bm2; S2, S-RNase from Nicotiana alata 24) ; RNS2, RNase from Arabidopsis thaliana 25) ; LE, RNase LE from Lycopersicon esculantum 26) ; MC1, RNase MC1 from bitter gourd 27) ; Oy, RNase Oy from oyster 28) ; DM, RNase from Drosophila melanogaster 29) ; RCL2, RNase from bullfrog, Rana Catesbeiana 30) ; CL1, RNase from chicken liver 31) ; BSP1, RNase from bovine spleen. The amino acid sequence deduced from the nucleotide sequence is shown in bold capital letters; the 3Ј-and 5Ј-flanking regions are shown in capital letters, and the intron is shown in lower-case letters.…”

On a Salmon (Onchorhynchus keta) Liver RNase, Belonging to RNase T2 Family: Primary Structure and Some Properties

“…1,2) Therefore, they are very easy to identify as to family and a good tool to study the evolution of RNases. In the animal kingdom, RNase T2 family enzymes have been studied mainly in animals belonging to vertebrates from mammals to amphibians [3][4][5][6] and two other lower animals. 7,8) The active sites of RNase T2 family enzymes have been studied mainly precisely on RNase Rh from Rhizopus niveus, RNase LE from cultured tomato (Lincopersicon esculentum), and RNase MC1 from bitter gourd (Momordica charantia), by enzymatically including site directed mutagenesis and X-ray crystallography.…”