Inosine-specific ribonuclease activity of natural variants of human endonuclease V

FEBS Lett. 2016 Dec;590(23):4354-4360. doi: 10.1002/1873-3468.12470. Epub 2016 Nov 14.

Abstract

Adenine bases in DNA, RNA, and nucleotides are deaminated during normal metabolism via hydrolytic and nitrosative reactions. In RNA, the deaminated product inosine is resolved by human endonuclease V, and mice deficient in this enzyme are cancer-prone. We have now produced, purified, and characterized naturally occurring variants of human endonuclease V (V29I, R112Q, K114R, H141Y, and D201N). We found that H141Y, but not other variants, is catalytically impaired, suggesting that individuals homozygous for H141Y may be predisposed to disease.

Keywords: RNA editing; endonuclease V; inosine.

Publication types

  • Letter

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biocatalysis
  • Homozygote
  • Humans
  • Inosine / metabolism*
  • Mutation*
  • Ribonucleases / chemistry
  • Ribonucleases / genetics*
  • Ribonucleases / metabolism*
  • Substrate Specificity

Substances

  • Inosine
  • Ribonucleases