Dual recognition-incision enzymes might be involved in mismatch repair and meiosis

Trends Biochem Sci. 2000 Sep;25(9):414-8. doi: 10.1016/s0968-0004(00)01623-6.

Abstract

Mismatch repair in many organisms depends on three proteins: the mismatch-recognition protein MutS, a nicking endonuclease MutH, and MutL, which acts as a scaffold between these. However, many genomes lack MutL but possess MutS. In one of these cases, in a coral mitochondrial genome, a gene is present that encodes a MutS protein fused to an HNH nicking endonuclease, potentially eliminating the requirement for MutL. Likewise, many prokaryotes could operate similarly, independently of MutL by encoding a fused MutS-Smr (MutS2) protein. Smr, which is proposed to be a nicking endonuclease, can also be found separately in many eukaryotes, where it might play a role in mismatch repair or meiotic chromosome crossing-over.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases*
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / physiology
  • Base Pair Mismatch*
  • Cnidaria / genetics
  • Cnidaria / metabolism
  • DNA / biosynthesis
  • DNA Repair*
  • DNA-Binding Proteins*
  • Escherichia coli Proteins*
  • Mitochondria / metabolism
  • Models, Genetic
  • Molecular Sequence Data
  • MutL Proteins
  • MutS DNA Mismatch-Binding Protein
  • Phylogeny
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • MutL protein, E coli
  • DNA
  • Adenosine Triphosphatases
  • MutL Proteins
  • MutS DNA Mismatch-Binding Protein
  • MutS protein, E coli