Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 584, Issue -, Pages 70-78Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2015.08.010
Keywords
Ribonuclease; Solution structure; RC-RNase 2; Base specificity; NMR
Categories
Funding
- Academia Sinica
- National Science Council
- National Taiwan University [NTU-ERP-101R8600-1, NTU-ICRP-102R7560-5]
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Cytotoxic ribonucleases found in the oocytes and early embryos of frogs with antitumor activity are well-documented. RC-RNase 2, a cytotoxic ribonuclease isolated from oocytes of bullfrog Rana catesbeiana, consists of 105 residues linked with 4 disulfide bridges and belongs to the bovine pancreatic ribonuclease (RNase A) superfamily. Among the RC-RNases, the base preference for RNase 2 is UpG but CpG for RC-RNase 4; while RC-RNase possesses the base specificity of both UpG and CpG. Interestingly, RC-RNase 2 or 4 has much lower catalytic activity but only three-fold less cytotoxicity than RC-RNase. Here, we report the NMR solution structure of rRC-RNase 2, comprising three alpha-helices and two sets of antiparallel beta-sheets. The differences of side-chain conformations of subsite residues among RNase A, RC-RNase, RC-RNase 4 and rRNase 2 are related to their distinct catalytic activities and base preferences. Furthermore, the substrate-related residues in the base specificity among native RC-RNases are derived using the chemical shift perturbation on ligand binding. (C) 2015 Elsevier Inc. All rights reserved.
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