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Are the effects of elevated temperature on meiotic recombination and thermotolerance linked via the axis and synaptonemal complex?

Christopher H MorganHuakun ZhangKirsten Bomblies
Published in: Philosophical transactions of the Royal Society of London. Series B, Biological sciences (2018)
Meiosis is unusual among cell divisions in shuffling genetic material by crossovers among homologous chromosomes and partitioning the genome into haploid gametes. Crossovers are critical for chromosome segregation in most eukaryotes, but are also an important factor in evolution, as they generate novel genetic combinations. The molecular mechanisms that underpin meiotic recombination and chromosome segregation are well conserved across kingdoms, but are also sensitive to perturbation by environment, especially temperature. Even subtle shifts in temperature can alter the number and placement of crossovers, while at greater extremes, structural failures can occur in the linear axis and synaptonemal complex structures which are essential for recombination and chromosome segregation. Understanding the effects of temperature on these processes is important for its implications in evolution and breeding, especially in the context of global warming. In this review, we first summarize the process of meiotic recombination and its reliance on axis and synaptonemal complex structures, and then discuss effects of temperature on these processes and structures. We hypothesize that some consistent effects of temperature on recombination and meiotic thermotolerance may commonly be two sides of the same coin, driven by effects of temperature on the folding or interaction of key meiotic proteins.This article is part of the themed issue 'Evolutionary causes and consequences of recombination rate variation in sexual organisms'.
Keyphrases
  • dna repair
  • dna damage
  • copy number
  • genome wide
  • high resolution
  • stem cells
  • oxidative stress
  • dna methylation
  • transcription factor
  • mesenchymal stem cells
  • bone marrow
  • molecular dynamics simulations
  • heat shock protein