UBR2 Mediates Transcriptional Silencing during Spermatogenesis via Histone Ubiquitination
Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases involved in histone ubiquitination, yet the responsible enzymes and the function of histone ubiquitination in spermatogenesis remain unclear....
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 107; no. 5; pp. 1912 - 1917 |
|---|---|
| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
02.02.2010
National Acad Sciences |
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| Online Access | Get full text |
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| Abstract | Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases involved in histone ubiquitination, yet the responsible enzymes and the function of histone ubiquitination in spermatogenesis remain unclear. We have previously shown that mice lacking the ubiquitin ligase UBR2, one of the recognition E3 components of the N-end rule proteolytic pathway, are infertile associated with meiotic arrest at prophase I. We here show that UBR2 localizes to meiotic chromatin regions, including unsynapsed axial elements linked to chromatin inactivation, and mediates transcriptional silencing via the ubiquitination of histone H2A. UBR2 interacts with the ubiquitin conjugating enzyme HR6B and its substrate H2A and promotes the HR6B-H2A interaction and the HR6B-to-H2A transfer of ubiquitin. UBR2 and ubiquitinated H2A (uH2A) spatiotemporally mark meiotic chromatin regions subject to transcriptional silencing, and UBR2-deficient spermatocytes fail to induce the ubiquitination of H2A during meiosis. UBR2-deficient spermatocytes are profoundly impaired in chromosomewide transcriptional silencing of genes linked to unsynapsed axes of the X and Y chromosomes. Our findings suggest that insufficiency in UBR2-dependent histone ubiquitination triggers a pachytene checkpoint system, providing a new insight into chromatin remodeling and gene expression regulation. |
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| AbstractList | Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases involved in histone ubiquitination, yet the responsible enzymes and the function of histone ubiquitination in spermatogenesis remain unclear. We have previously shown that mice lacking the ubiquitin ligase UBR2, one of the recognition E3 components of the N-end rule proteolytic pathway, are infertile associated with meiotic arrest at prophase I. We here show that UBR2 localizes to meiotic chromatin regions, including unsynapsed axial elements linked to chromatin inactivation, and mediates transcriptional silencing via the ubiquitination of histone H2A. UBR2 interacts with the ubiquitin conjugating enzyme HR6B and its substrate H2A and promotes the HR6B-H2A interaction and the HR6B-to-H2A transfer of ubiquitin. UBR2 and ubiquitinated H2A (uH2A) spatiotemporally mark meiotic chromatin regions subject to transcriptional silencing, and UBR2-deficient spermatocytes fail to induce the ubiquitination of H2A during meiosis. UBR2-deficient spermatocytes are profoundly impaired in chromosomewide transcriptional silencing of genes linked to unsynapsed axes of the X and Y chromosomes. Our findings suggest that insufficiency in UBR2-dependent histone ubiquitination triggers a pachytene checkpoint system, providing a new insight into chromatin remodeling and gene expression regulation. Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases involved in histone ubiquitination, yet the responsible enzymes and the function of histone ubiquitination in spermatogenesis remain unclear. We have previously shown that mice lacking the ubiquitin ligase UBR2, one of the recognition E3 components of the N-end rule proteolytic pathway, are infertile associated with meiotic arrest at prophase I. We here show that UBR2 localizes to meiotic chromatin regions, including unsynapsed axial elements linked to chromatin inactivation, and mediates transcriptional silencing via the ubiquitination of histone H2A. UBR2 interacts with the ubiquitin conjugating enzyme HR6B and its substrate H2A and promotes the HR6B–H2A interaction and the HR6B-to-H2A transfer of ubiquitin. UBR2 and ubiquitinated H2A (uH2A) spatiotemporally mark meiotic chromatin regions subject to transcriptional silencing, and UBR2-deficient spermatocytes fail to induce the ubiquitination of H2A during meiosis. UBR2-deficient spermatocytes are profoundly impaired in chromosome-wide transcriptional silencing of genes linked to unsynapsed axes of the X and Y chromosomes. Our findings suggest that insufficiency in UBR2-dependent histone ubiquitination triggers a pachytene checkpoint system, providing a new insight into chromatin remodeling and gene expression regulation. Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases involved in histone ubiquitination, yet the responsible enzymes and the function of histone ubiquitination in spermatogenesis remain unclear. We have previously shown that mice lacking the ubiquitin ligase UBR2, one of the recognition E3 components of the N-end rule proteolytic pathway, are infertile associated with meiotic arrest at prophase I. We here show that UBR2 localizes to meiotic chromatin regions, including unsynapsed axial elements linked to chromatin inactivation, and mediates transcriptional silencing via the ubiquitination of histone H2A. UBR2 interacts with the ubiquitin conjugating enzyme HR6B and its substrate H2A and promotes the HR6B - H2A interaction and the HR6B-to-H2A transfer of ubiquitin. UBR2 and ubiquitinated H2A (uH2A) spatiotemporally mark meiotic chromatin regions subject to transcriptional silencing, and UBR2-deficient spermatocytes fail to induce the ubiquitination of H2A during meiosis. UBR2-deficient spermatocytes are profoundly impaired in chromosome-wide transcriptional silencing of genes linked to unsynapsed axes of the X and Y chromosomes. Our findings suggest that insufficiency in UBR2-dependent histone ubiquitination triggers a pachytene checkpoint system, providing a new insight into chromatin remodeling and gene expression regulation. [PUBLICATION ABSTRACT] Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases involved in histone ubiquitination, yet the responsible enzymes and the function of histone ubiquitination in spermatogenesis remain unclear. We have previously shown that mice lacking the ubiquitin ligase UBR2, one of the recognition E3 components of the N-end rule proteolytic pathway, are infertile associated with meiotic arrest at prophase I. We here show that UBR2 localizes to meiotic chromatin regions, including unsynapsed axial elements linked to chromatin inactivation, and mediates transcriptional silencing via the ubiquitination of histone H2A. UBR2 interacts with the ubiquitin conjugating enzyme HR6B and its substrate H2A and promotes the HR6B-H2A interaction and the HR6B-to-H2A transfer of ubiquitin. UBR2 and ubiquitinated H2A (uH2A) spatiotemporally mark meiotic chromatin regions subject to transcriptional silencing, and UBR2-deficient spermatocytes fail to induce the ubiquitination of H2A during meiosis. UBR2-deficient spermatocytes are profoundly impaired in chromosome-wide transcriptional silencing of genes linked to unsynapsed axes of the X and Y chromosomes. Our findings suggest that insufficiency in UBR2-dependent histone ubiquitination triggers a pachytene checkpoint system, providing a new insight into chromatin remodeling and gene expression regulation.Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases involved in histone ubiquitination, yet the responsible enzymes and the function of histone ubiquitination in spermatogenesis remain unclear. We have previously shown that mice lacking the ubiquitin ligase UBR2, one of the recognition E3 components of the N-end rule proteolytic pathway, are infertile associated with meiotic arrest at prophase I. We here show that UBR2 localizes to meiotic chromatin regions, including unsynapsed axial elements linked to chromatin inactivation, and mediates transcriptional silencing via the ubiquitination of histone H2A. UBR2 interacts with the ubiquitin conjugating enzyme HR6B and its substrate H2A and promotes the HR6B-H2A interaction and the HR6B-to-H2A transfer of ubiquitin. UBR2 and ubiquitinated H2A (uH2A) spatiotemporally mark meiotic chromatin regions subject to transcriptional silencing, and UBR2-deficient spermatocytes fail to induce the ubiquitination of H2A during meiosis. UBR2-deficient spermatocytes are profoundly impaired in chromosome-wide transcriptional silencing of genes linked to unsynapsed axes of the X and Y chromosomes. Our findings suggest that insufficiency in UBR2-dependent histone ubiquitination triggers a pachytene checkpoint system, providing a new insight into chromatin remodeling and gene expression regulation. |
| Author | Jiang, Yonghua Mook-Jung, Inhee Kwon, Yong Tae Young, Jee Lee, Min Jae Kim, Dong Eun Varshavsky, Alexander Zakrzewska, Adriana Zhang, Yi Kirn, Eun-A. |
| Author_xml | – sequence: 1 givenname: Jee surname: Young fullname: Young, Jee – sequence: 2 givenname: Eun-A. surname: Kirn fullname: Kirn, Eun-A. – sequence: 3 givenname: Yonghua surname: Jiang fullname: Jiang, Yonghua – sequence: 4 givenname: Adriana surname: Zakrzewska fullname: Zakrzewska, Adriana – sequence: 5 givenname: Dong Eun surname: Kim fullname: Kim, Dong Eun – sequence: 6 givenname: Min Jae surname: Lee fullname: Lee, Min Jae – sequence: 7 givenname: Inhee surname: Mook-Jung fullname: Mook-Jung, Inhee – sequence: 8 givenname: Yi surname: Zhang fullname: Zhang, Yi – sequence: 9 givenname: Yong Tae surname: Kwon fullname: Kwon, Yong Tae – sequence: 10 givenname: Alexander surname: Varshavsky fullname: Varshavsky, Alexander |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20080676$$D View this record in MEDLINE/PubMed |
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| Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 1J.Y.A., E.-A. K., and Y.J. contributed equally to this work. Edited by Alexander Varshavsky, California Institute of Technology, Pasadena, CA, and approved November 6, 2009 (received for review September 9, 2009) Author contributions: J.Y.A., E.-A. K., Y.J., M.J.L., I.M.-J., and Y.T.K. designed research; J.Y.A., E.-A. K., Y.J., A.Z., D.E.K., and M.J.L. performed research; Y.Z. contributed new reagents/analytic tools; J.Y.A., E.-A. K., Y.J., D.E.K., M.J.L., I.M.-J., Y.Z., and Y.T.K. analyzed data; and J.Y.A., E.-A. K., Y.J., and Y.T.K. wrote the paper. |
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| Snippet | Ubiquitination of histones provides an important mechanism regulating chromatin remodeling and gene expression. Recent studies have revealed ubiquitin ligases... |
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| SubjectTerms | Animals Biological Sciences Chromatin Chromatin - genetics Chromatin - metabolism Chromatin Assembly and Disassembly - genetics Chromatin Assembly and Disassembly - physiology Chromosomes Enzymes Gene expression gene expression regulation Gene Silencing - physiology Genes Histones Histones - chemistry Histones - metabolism Humans Inactivation Male Meiosis Meiosis - genetics Meiosis - physiology Mice Mice, Knockout Models, Biological Pachytene stage proteolysis Sex chromosomes Spermatocytes Spermatocytes - metabolism spermatogenesis Spermatogenesis - genetics Spermatogenesis - physiology Testes transcription (genetics) ubiquitin Ubiquitin-Conjugating Enzymes - metabolism ubiquitin-protein ligase Ubiquitin-Protein Ligases - deficiency Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination Ubiquitins X Chromosome - genetics X Chromosome - metabolism Y chromosome Y Chromosome - genetics Y Chromosome - metabolism |
| Title | UBR2 Mediates Transcriptional Silencing during Spermatogenesis via Histone Ubiquitination |
| URI | https://www.jstor.org/stable/40536508 http://www.pnas.org/content/107/5/1912.abstract https://www.ncbi.nlm.nih.gov/pubmed/20080676 https://www.proquest.com/docview/201434721 https://www.proquest.com/docview/46539935 https://www.proquest.com/docview/733618034 https://pubmed.ncbi.nlm.nih.gov/PMC2836623 |
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