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The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis

Homologous recombination in meiosis is initiated by the programmed induction of double strand breaks (DSBs). Although the Drosophila Spo11 ortholog Mei-W68 is required for the induction of DSBs during meiotic prophase, only one other protein (Mei-P22) has been shown to be required for Mei-W68 to exe...

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Detalles Bibliográficos
Autores principales: Lake, Cathleen M., Nielsen, Rachel J., Hawley, R. Scott
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044681/
https://www.ncbi.nlm.nih.gov/pubmed/21383963
http://dx.doi.org/10.1371/journal.pgen.1002005
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author Lake, Cathleen M.
Nielsen, Rachel J.
Hawley, R. Scott
author_facet Lake, Cathleen M.
Nielsen, Rachel J.
Hawley, R. Scott
author_sort Lake, Cathleen M.
collection PubMed
description Homologous recombination in meiosis is initiated by the programmed induction of double strand breaks (DSBs). Although the Drosophila Spo11 ortholog Mei-W68 is required for the induction of DSBs during meiotic prophase, only one other protein (Mei-P22) has been shown to be required for Mei-W68 to exert this function. We show here that the chromatin-associated protein Trade Embargo (Trem), a C2H2 zinc finger protein, is required to localize Mei-P22 to discrete foci on meiotic chromosomes, and thus to promote the formation of DSBs, making Trem the earliest known function in the process of DSB formation in Drosophila oocytes. We speculate that Trem may act by either directing the binding of Mei-P22 to preferred sites of DSB formation or by altering chromatin structure in a manner that allows Mei-P22 to form foci.
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spelling pubmed-30446812011-03-07 The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis Lake, Cathleen M. Nielsen, Rachel J. Hawley, R. Scott PLoS Genet Research Article Homologous recombination in meiosis is initiated by the programmed induction of double strand breaks (DSBs). Although the Drosophila Spo11 ortholog Mei-W68 is required for the induction of DSBs during meiotic prophase, only one other protein (Mei-P22) has been shown to be required for Mei-W68 to exert this function. We show here that the chromatin-associated protein Trade Embargo (Trem), a C2H2 zinc finger protein, is required to localize Mei-P22 to discrete foci on meiotic chromosomes, and thus to promote the formation of DSBs, making Trem the earliest known function in the process of DSB formation in Drosophila oocytes. We speculate that Trem may act by either directing the binding of Mei-P22 to preferred sites of DSB formation or by altering chromatin structure in a manner that allows Mei-P22 to form foci. Public Library of Science 2011-02-24 /pmc/articles/PMC3044681/ /pubmed/21383963 http://dx.doi.org/10.1371/journal.pgen.1002005 Text en Lake et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Lake, Cathleen M.
Nielsen, Rachel J.
Hawley, R. Scott
The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis
title The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis
title_full The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis
title_fullStr The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis
title_full_unstemmed The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis
title_short The Drosophila Zinc Finger Protein Trade Embargo Is Required for Double Strand Break Formation in Meiosis
title_sort drosophila zinc finger protein trade embargo is required for double strand break formation in meiosis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044681/
https://www.ncbi.nlm.nih.gov/pubmed/21383963
http://dx.doi.org/10.1371/journal.pgen.1002005
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