Meiotic recombination cold spots in chromosomal cohesion sites. 2014

Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
Department of Life Sciences, The University of Tokyo, Komaba 3-8-1, Meguro-ku, Tokyo 153-8902, Japan.

Meiotic chromosome architecture called 'axis-loop structures' and histone modifications have been shown to regulate the Spo11-dependent formation of DNA double-strand breaks (DSBs) that trigger meiotic recombination. Using genome-wide chromatin immunoprecipitation (ChIP) analyses followed by deep sequencing, we compared the genome-wide distribution of the axis protein Rec8 (the kleisin subunit of meiotic cohesin) with that of oligomeric DNA covalently bound to Spo11, indicative of DSB sites. The frequency of DSB sites is overall constant between Rec8 binding sites. However, DSB cold spots are observed in regions spanning ±0.8 kb around Rec8 binding sites. The axis-associated cold spots are not due to the exclusion of Spo11 localization from the axis, because ChIP experiments showed that substantial Spo11 persists at Rec8 binding sites during DSB formation. Spo11 fused with Gal4 DNA binding domain (Gal4BD-Spo11) tethered in close proximity (≤0.8 kb) to Rec8 binding sites hardly forms meiotic DSBs, in contrast with other regions. In addition, H3K4 trimethylation (H3K4me3) remarkably decreases at Rec8 binding sites. These results suggest that reduced histone H3K4me3 in combination with inactivation of Spo11 activity on the axis discourages DSB hot spot formation.

UI MeSH Term Description Entries
D008540 Meiosis A type of CELL NUCLEUS division, occurring during maturation of the GERM CELLS. Two successive cell nucleus divisions following a single chromosome duplication (S PHASE) result in daughter cells with half the number of CHROMOSOMES as the parent cells. M Phase, Meiotic,Meiotic M Phase,M Phases, Meiotic,Meioses,Meiotic M Phases,Phase, Meiotic M,Phases, Meiotic M
D008745 Methylation Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed) Methylations
D011995 Recombination, Genetic Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses. Genetic Recombination,Recombination,Genetic Recombinations,Recombinations,Recombinations, Genetic
D002842 Chromatids Either of the two longitudinally adjacent threads formed when a eukaryotic chromosome replicates prior to mitosis. The chromatids are held together at the centromere. Sister chromatids are derived from the same chromosome. (Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed) Chromatid
D002868 Chromosomal Proteins, Non-Histone Nucleoproteins, which in contrast to HISTONES, are acid insoluble. They are involved in chromosomal functions; e.g. they bind selectively to DNA, stimulate transcription resulting in tissue-specific RNA synthesis and undergo specific changes in response to various hormones or phytomitogens. Non-Histone Chromosomal Proteins,Chromosomal Proteins, Non Histone,Chromosomal Proteins, Nonhistone,Non-Histone Chromosomal Phosphoproteins,Chromosomal Phosphoproteins, Non-Histone,Non Histone Chromosomal Phosphoproteins,Non Histone Chromosomal Proteins,Nonhistone Chromosomal Proteins,Proteins, Non-Histone Chromosomal
D004706 Endodeoxyribonucleases A group of enzymes catalyzing the endonucleolytic cleavage of DNA. They include members of EC 3.1.21.-, EC 3.1.22.-, EC 3.1.23.- (DNA RESTRICTION ENZYMES), EC 3.1.24.- (DNA RESTRICTION ENZYMES), and EC 3.1.25.-.
D006657 Histones Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each. Histone,Histone H1,Histone H1(s),Histone H2a,Histone H2b,Histone H3,Histone H3.3,Histone H4,Histone H5,Histone H7
D000097722 Cohesins Protein complex constituents that bind chromosomes from late G1 until the metaphase - anaphase transition. The cohesin complex regulates sister chromatid cohesion, HOMOLOGOUS RECOMBINATION and DNA looping. Cohesin,Cohesin Protein Complex
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker

Related Publications

Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
May 2001, Nature reviews. Genetics,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
January 2007, Annual review of genetics,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
March 2006, Cell cycle (Georgetown, Tex.),
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
January 2006, BioEssays : news and reviews in molecular, cellular and developmental biology,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
January 2011, PloS one,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
October 2015, Genes & development,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
September 2003, Trends in genetics : TIG,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
February 2019, Journal of bioscience and bioengineering,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
January 2004, Philosophical transactions of the Royal Society of London. Series B, Biological sciences,
Masaru Ito, and Kazuto Kugou, and Jeffrey A Fawcett, and Sachiko Mura, and Sho Ikeda, and Hideki Innan, and Kunihiro Ohta
January 2006, Nucleic acids research,
Copied contents to your clipboard!