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[Structures and functions of ribonucleases]

M Irie1

  • 1Department of Microbiology, Hoshi College of Pharmacy, Tokyo, Japan.

Yakugaku Zasshi : Journal of the Pharmaceutical Society of Japan
|November 14, 1997
PubMed
Summary
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This study investigates the structure and function of various RNases, including bovine pancreatic RNase A and newly discovered fungal and animal enzymes. Researchers elucidated catalytic mechanisms and identified key amino acid residues responsible for base specificity, enabling artificial modification of enzyme behavior.

Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Structural Biology

Context:

  • Understanding ribonuclease (RNase) structure-function relationships is crucial for various biotechnological applications.
  • Bovine pancreatic RNase A serves as a model enzyme, but diverse RNases with unique properties exist across species and kingdoms.
  • Elucidating the catalytic mechanisms and substrate specificities of these enzymes is essential for their effective utilization.

Purpose:

  • To investigate the subsite structure and kinetic properties of bovine pancreatic RNase A.
  • To isolate, characterize, and determine the primary structures of novel RNases from different sources.
  • To elucidate the catalytic mechanisms and base recognition sites of specific RNases, including RNase Rh.

Summary:

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  • Kinetic and crystallographic studies revealed the subsite structure of bovine pancreatic RNase A, identifying Lys66, Lys7, and Lys1 as key residues.
  • New pyrimidine-specific RNases were isolated, including a heat-stable bullfrog liver RNase and a bovine brain RNase with unique modifications.
  • RNases from Aspergillus saitoi and a mushroom were characterized as belonging to the RNase T1 family, with insights into their catalytic mechanisms.
  • Several fungal, plant, and animal RNases were classified as RNase T2 family, with identified catalytic sites (His46, His104, His109, Glu105, Lys108) and base recognition sites (Asp51, Trp49, Tyr57) in RNase Rh.
  • Protein engineering studies demonstrated the ability to artificially alter the base specificity of RNase Rh by modifying key amino acid residues.

    • Impact:

    • Provides detailed insights into the molecular basis of RNase activity and substrate specificity.
    • Expands the known diversity of RNase enzymes and their structural/functional characteristics.
    • Demonstrates the potential for engineering RNases with tailored specificities for biotechnological applications.