Localization of MMR proteins on meiotic chromosomes in mice indicates distinct functions during prophase I. Academic Article uri icon

Overview

MeSH

  • Adaptor Proteins, Signal Transducing
  • Adenosine Triphosphatases
  • Animals
  • Cell Cycle Proteins
  • Centromere
  • DNA Repair Enzymes
  • DNA-Binding Proteins
  • Male
  • Meiosis
  • Mice
  • Mice, Knockout
  • Microscopy, Immunoelectron
  • Mismatch Repair Endonuclease PMS2
  • MutL Protein Homolog 1
  • MutL Proteins
  • Nuclear Proteins
  • Protein Binding
  • Proteins
  • Spermatocytes

MeSH Major

  • Carrier Proteins
  • Meiotic Prophase I
  • MutS Homolog 2 Protein
  • Y Chromosome

abstract

  • Mammalian MutL homologues function in DNA mismatch repair (MMR) after replication errors and in meiotic recombination. Both functions are initiated by a heterodimer of MutS homologues specific to either MMR (MSH2-MSH3 or MSH2-MSH6) or crossing over (MSH4-MSH5). Mutations of three of the four MutL homologues (Mlh1, Mlh3, and Pms2) result in meiotic defects. We show herein that two distinct complexes involving MLH3 are formed during murine meiosis. The first is a stable association between MLH3 and MLH1 and is involved in promoting crossing over in conjunction with MSH4-MSH5. The second complex involves MLH3 together with MSH2-MSH3 and localizes to repetitive sequences at centromeres and the Y chromosome. This complex is up-regulated in Pms2-/- males, but not females, providing an explanation for the sexual dimorphism seen in Pms2-/- mice. The association of MLH3 with repetitive DNA sequences is coincident with MSH2-MSH3 and is decreased in Msh2-/- and Msh3-/- mice, suggesting a novel role for the MMR family in the maintenance of repeat unit integrity during mammalian meiosis.

publication date

  • November 7, 2005

has subject area

  • Adaptor Proteins, Signal Transducing
  • Adenosine Triphosphatases
  • Animals
  • Carrier Proteins
  • Cell Cycle Proteins
  • Centromere
  • DNA Repair Enzymes
  • DNA-Binding Proteins
  • Male
  • Meiosis
  • Meiotic Prophase I
  • Mice
  • Mice, Knockout
  • Microscopy, Immunoelectron
  • Mismatch Repair Endonuclease PMS2
  • MutL Protein Homolog 1
  • MutL Proteins
  • MutS Homolog 2 Protein
  • Nuclear Proteins
  • Protein Binding
  • Proteins
  • Spermatocytes
  • Y Chromosome

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2171243

Digital Object Identifier (DOI)

  • 10.1083/jcb.200506170

PubMed ID

  • 16260499

Additional Document Info

start page

  • 447

end page

  • 458

volume

  • 171

number

  • 3