Mammalian-specific sequences in pou3f2 contribute to maternal behavior

Genome Biol Evol. 2014 Apr 7;6(5):1145-56. doi: 10.1093/gbe/evu072.

Abstract

Various mutations have occurred during evolution among orthologs, genes in different species that diverged from a common ancestral gene by speciation. Here, we report the remarkable deterioration of a characteristic mammalian maternal behavior, pup retrieval, in nonmammalized mice, in which the transcription factor Pou3f2 was replaced with the Xenopus ortholog lacking all of the homopolymeric amino acid repeats of mammalian POU3F2. Most of the pups born to the nonmammalized mice died within days after birth, depending on the dam genotype alone. Quantitative immunohistochemical analysis revealed decreases in the rate-limiting enzymes of dopamine and serotonin synthesis in various brain structures. Similar results were obtained in knock-in mice in which all of the homopolymeric amino acid repeats of mammalian POU3F2 were removed. Pup retrieval behavior in mammals is thus strongly related to monoamine neurotransmitter levels via the acquisition of homopolymeric amino acid repeats during mammalian evolution.

Keywords: Pou3f2/Brn-2; amino acid repeats; maternal behavior; nonmammalized mice; transcription factor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Newborn
  • Behavior, Animal / physiology
  • Brain / metabolism*
  • Dopamine / biosynthesis
  • Female
  • Gene Knock-In Techniques
  • Mammals / genetics*
  • Maternal Behavior / physiology*
  • Mice, Mutant Strains
  • Nerve Tissue Proteins / genetics*
  • Nerve Tissue Proteins / metabolism
  • POU Domain Factors / genetics*
  • POU Domain Factors / metabolism
  • Repetitive Sequences, Amino Acid
  • Serotonin / biosynthesis
  • Tryptophan Hydroxylase / metabolism
  • Tyrosine 3-Monooxygenase / metabolism
  • Xenopus Proteins / genetics

Substances

  • Nerve Tissue Proteins
  • POU Domain Factors
  • Xenopus Proteins
  • Pou3f2 protein, mouse
  • Serotonin
  • Tyrosine 3-Monooxygenase
  • Tph2 protein, mouse
  • Tryptophan Hydroxylase
  • Dopamine