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Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay
RATIONALE: Post‐translational modifications (PTMs) of histones result in changes to transcriptional activities and chromatin remodeling. Lysine 9 of histone H3 (H3K9) is subject to PTMs, such as methylation and acetylation, which influence histone activity during spermatogenesis. Characterization st...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5108415/ https://www.ncbi.nlm.nih.gov/pubmed/27643486 http://dx.doi.org/10.1002/rcm.7742 |
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author | Kwak, Ho‐Geun Dohmae, Naoshi |
author_facet | Kwak, Ho‐Geun Dohmae, Naoshi |
author_sort | Kwak, Ho‐Geun |
collection | PubMed |
description | RATIONALE: Post‐translational modifications (PTMs) of histones result in changes to transcriptional activities and chromatin remodeling. Lysine 9 of histone H3 (H3K9) is subject to PTMs, such as methylation and acetylation, which influence histone activity during spermatogenesis. Characterization strategies for studying PTMs on H3K9 have been developed to provide epigenetic and proteomic information. Proteomic analysis has been used to limited success to study PTMs on H3K9; however, a comprehensive analytical approach is required to elucidate global patterns of PTMs of H3 variants during spermatogenesis. METHODS: Intact H3 variants in mouse testis were separated by high‐performance liquid chromatography on a reversed‐phase column with an ion‐pairing reagent. Modifications to H3K9 were identified via top‐down analysis using matrix‐assisted laser desorption/ionization in source decay (MALDI‐ISD). RESULTS: Mono‐, di‐, and tri‐methylations were identified at H3K9 in mouse testis and epididymis. These modifications were also observed in testis‐specific histone H3 (H3t). Specifically, tri‐methylation was more abundant on H3tK9 than on K9 of other H3 variants. CONCLUSIONS: We introduce a method for rapid, simple, and comprehensive characterization of PTMs on the N‐termini of H3 variants using MALDI‐ISD. This approach provides novel and useful information, including K9 modifications on H3t, which would benefit epigenetic and proteomic research. © 2016 The Authors. Rapid Communications in Mass Spectrometry Published by John Wiley & Sons Ltd. |
format | Online Article Text |
id | pubmed-5108415 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-51084152016-11-16 Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay Kwak, Ho‐Geun Dohmae, Naoshi Rapid Commun Mass Spectrom Research Articles RATIONALE: Post‐translational modifications (PTMs) of histones result in changes to transcriptional activities and chromatin remodeling. Lysine 9 of histone H3 (H3K9) is subject to PTMs, such as methylation and acetylation, which influence histone activity during spermatogenesis. Characterization strategies for studying PTMs on H3K9 have been developed to provide epigenetic and proteomic information. Proteomic analysis has been used to limited success to study PTMs on H3K9; however, a comprehensive analytical approach is required to elucidate global patterns of PTMs of H3 variants during spermatogenesis. METHODS: Intact H3 variants in mouse testis were separated by high‐performance liquid chromatography on a reversed‐phase column with an ion‐pairing reagent. Modifications to H3K9 were identified via top‐down analysis using matrix‐assisted laser desorption/ionization in source decay (MALDI‐ISD). RESULTS: Mono‐, di‐, and tri‐methylations were identified at H3K9 in mouse testis and epididymis. These modifications were also observed in testis‐specific histone H3 (H3t). Specifically, tri‐methylation was more abundant on H3tK9 than on K9 of other H3 variants. CONCLUSIONS: We introduce a method for rapid, simple, and comprehensive characterization of PTMs on the N‐termini of H3 variants using MALDI‐ISD. This approach provides novel and useful information, including K9 modifications on H3t, which would benefit epigenetic and proteomic research. © 2016 The Authors. Rapid Communications in Mass Spectrometry Published by John Wiley & Sons Ltd. John Wiley and Sons Inc. 2016-10-20 2016-12-15 /pmc/articles/PMC5108415/ /pubmed/27643486 http://dx.doi.org/10.1002/rcm.7742 Text en © 2016 The Authors. Rapid Communications in Mass Spectrometry Published by John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial (http://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Research Articles Kwak, Ho‐Geun Dohmae, Naoshi Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay |
title | Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay |
title_full | Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay |
title_fullStr | Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay |
title_full_unstemmed | Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay |
title_short | Characterization of post‐translational modifications on lysine 9 of histone H3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay |
title_sort | characterization of post‐translational modifications on lysine 9 of histone h3 variants in mouse testis using matrix‐assisted laser desorption/ionization in‐source decay |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5108415/ https://www.ncbi.nlm.nih.gov/pubmed/27643486 http://dx.doi.org/10.1002/rcm.7742 |
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