Methylation of H2AR29 is a novel repressive PRMT6 target.
BACKGROUND: Covalent histone modifications are central to all DNA-dependent processes. Modifications of histones H3 and H4 are becoming well characterised, but knowledge of how H2A modifications regulate chromatin dynamics and gene expression is still very limited. RESULTS: To understand the functi...
Main Authors: | , , , , , , , , , , |
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Format: | Journal article |
Language: | English |
Published: |
2011
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author | Waldmann, T Izzo, A Kamieniarz, K Richter, F Vogler, C Sarg, B Lindner, H Young, N Mittler, G Garcia, B Schneider, R |
author_facet | Waldmann, T Izzo, A Kamieniarz, K Richter, F Vogler, C Sarg, B Lindner, H Young, N Mittler, G Garcia, B Schneider, R |
author_sort | Waldmann, T |
collection | OXFORD |
description | BACKGROUND: Covalent histone modifications are central to all DNA-dependent processes. Modifications of histones H3 and H4 are becoming well characterised, but knowledge of how H2A modifications regulate chromatin dynamics and gene expression is still very limited. RESULTS: To understand the function of H2A modifications, we performed a systematic analysis of the histone H2A methylation status. We identified and functionally characterised two new methylation sites in H2A: R11 (H2AR11) and R29 (H2AR29). Using an unbiased biochemical approach in combination with candidate assays we showed that protein arginine methyltransferase (PRMT) 1 and PRMT6 are unique in their ability to catalyse these modifications. Importantly we found that H2AR29me2 is specifically enriched at genes repressed by PRMT6, implicating H2AR29me2 in transcriptional repression. CONCLUSIONS: Our data establishes R11 and R29 as new arginine methylation sites in H2A. We identified the specific modifying enzymes involved, and uncovered a novel functional role of H2AR29me2 in gene silencing in vivo. Thus this work reveals novel insights into the function of H2A methylation and in the mechanisms of PRMT6-mediated transcriptional repression. |
first_indexed | 2024-03-07T01:58:50Z |
format | Journal article |
id | oxford-uuid:9ca9f729-b861-46b6-9b35-ed946079ca28 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T01:58:50Z |
publishDate | 2011 |
record_format | dspace |
spelling | oxford-uuid:9ca9f729-b861-46b6-9b35-ed946079ca282022-03-27T00:37:30ZMethylation of H2AR29 is a novel repressive PRMT6 target.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:9ca9f729-b861-46b6-9b35-ed946079ca28EnglishSymplectic Elements at Oxford2011Waldmann, TIzzo, AKamieniarz, KRichter, FVogler, CSarg, BLindner, HYoung, NMittler, GGarcia, BSchneider, R BACKGROUND: Covalent histone modifications are central to all DNA-dependent processes. Modifications of histones H3 and H4 are becoming well characterised, but knowledge of how H2A modifications regulate chromatin dynamics and gene expression is still very limited. RESULTS: To understand the function of H2A modifications, we performed a systematic analysis of the histone H2A methylation status. We identified and functionally characterised two new methylation sites in H2A: R11 (H2AR11) and R29 (H2AR29). Using an unbiased biochemical approach in combination with candidate assays we showed that protein arginine methyltransferase (PRMT) 1 and PRMT6 are unique in their ability to catalyse these modifications. Importantly we found that H2AR29me2 is specifically enriched at genes repressed by PRMT6, implicating H2AR29me2 in transcriptional repression. CONCLUSIONS: Our data establishes R11 and R29 as new arginine methylation sites in H2A. We identified the specific modifying enzymes involved, and uncovered a novel functional role of H2AR29me2 in gene silencing in vivo. Thus this work reveals novel insights into the function of H2A methylation and in the mechanisms of PRMT6-mediated transcriptional repression. |
spellingShingle | Waldmann, T Izzo, A Kamieniarz, K Richter, F Vogler, C Sarg, B Lindner, H Young, N Mittler, G Garcia, B Schneider, R Methylation of H2AR29 is a novel repressive PRMT6 target. |
title | Methylation of H2AR29 is a novel repressive PRMT6 target. |
title_full | Methylation of H2AR29 is a novel repressive PRMT6 target. |
title_fullStr | Methylation of H2AR29 is a novel repressive PRMT6 target. |
title_full_unstemmed | Methylation of H2AR29 is a novel repressive PRMT6 target. |
title_short | Methylation of H2AR29 is a novel repressive PRMT6 target. |
title_sort | methylation of h2ar29 is a novel repressive prmt6 target |
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