Structures, Mechanisms, and Functions of His-Me Finger Nucleases

Trends Biochem Sci. 2020 Nov;45(11):935-946. doi: 10.1016/j.tibs.2020.07.002. Epub 2020 Aug 14.

Abstract

His-Me finger (also called HNH or ββα-me) nucleases, are a large superfamily of nucleases that share limited sequence homology, but all members carry a highly similar catalytic motif exhibiting a ββα topology. This review represents a structural comparison of His-Me finger nucleases, summarizing their substrate-binding and recognition strategies, mechanisms of enzymatic hydrolysis, cellular functions, and the various means of activity regulation. His-Me finger nucleases usually function as monomers, making a single nick in nucleic acids to degrade foreign or host genomes, or as homodimers that introduce double-stranded DNA breaks for DNA restriction, integration, recombination, and repair. Various cellular neutralizing machineries have evolved to regulate the activity of His-Me finger nucleases, thereby maintaining genome integrity and cellular functionality.

Keywords: DNA cleavage; DNA hydrolysis; DNase; HNH family.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biocatalysis
  • Endonucleases / chemistry*
  • Endonucleases / genetics
  • Endonucleases / metabolism*
  • Humans
  • Models, Molecular
  • Protein Conformation

Substances

  • Endonucleases