Structure-function relationships of acid ribonucleases: lysosomal, vacuolar, and periplasmic enzymes

Pharmacol Ther. 1999 Feb;81(2):77-89. doi: 10.1016/s0163-7258(98)00035-7.

Abstract

It is surprising that only relatively recently has attention been directed to the characterization of the properties of acid ribonucleases (RNases), leading to some understanding of their biochemistry and their functional roles. The present review summarizes current progress in this field under the following general topics: (1) the wide distribution of acid RNases in organisms from viruses to animals; (2) recent findings concerning their primary and three-dimensional structure; (3) the structure-function relationship of acid RNases, with a fungal RNase from Rhizopus niveus as a model enzyme; (4) the unique localization of acid RNases in the periplasm of bacteria, vacuoles in plants, and lysosomes of animals and protozoa; and (5) the diversity of physiological roles, depending on the organism, such as self-incompatibility factors and defense proteins in some plants, the surface protein of an animal virus related to pathogenicity, and possible relationship to human cancer.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacteria / enzymology
  • Fungi / enzymology
  • Humans
  • Molecular Conformation
  • Molecular Sequence Data
  • Plants / enzymology
  • Ribonucleases / chemistry*
  • Ribonucleases / physiology*
  • Structure-Activity Relationship
  • Viruses / enzymology

Substances

  • Ribonucleases