Biochemical Analysis of Histone Succinylation
Posttranslational modification (PTM) of proteins is used to regulate protein activity and stability. Histone PTMs are regarded as some of the most important, as they can directly regulate gene expression through chromatin reorganization. Recently, histone proteins were found to undergo succinylation...
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| Format: | Article |
| Language: | English |
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Wiley
2017-01-01
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| Series: | Biochemistry Research International |
| Online Access: | http://dx.doi.org/10.1155/2017/8529404 |
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| author | Atsushi Yokoyama Shogo Katsura Akira Sugawara |
| author_facet | Atsushi Yokoyama Shogo Katsura Akira Sugawara |
| author_sort | Atsushi Yokoyama |
| collection | DOAJ |
| description | Posttranslational modification (PTM) of proteins is used to regulate protein activity and stability. Histone PTMs are regarded as some of the most important, as they can directly regulate gene expression through chromatin reorganization. Recently, histone proteins were found to undergo succinylation, adding to other well-known PTMs such as acetylation, methylation, and phosphorylation. However, there is little information regarding the enzyme which catalyzes histone lysine succinylation. In fact, it is unclear whether this reaction is enzymatic. In this study, we tested histone succinylation activity in vitro using cell nuclear extracts of HepG2 cells. Although whole nuclear extracts did not show histone succinylation activity, we found that an SP 1.0 M KCl fraction of nuclear extracts indeed had such activity. These data offer the first direct evidence that histone succinylation is an enzymatic PTM as are other histone codes in the nucleus. |
| format | Article |
| id | doaj-art-23461646194b47939a3e634abcc7ca39 |
| institution | Kabale University |
| issn | 2090-2247 2090-2255 |
| language | English |
| publishDate | 2017-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Biochemistry Research International |
| spelling | doaj-art-23461646194b47939a3e634abcc7ca392025-02-03T05:48:01ZengWileyBiochemistry Research International2090-22472090-22552017-01-01201710.1155/2017/85294048529404Biochemical Analysis of Histone SuccinylationAtsushi Yokoyama0Shogo Katsura1Akira Sugawara2Department of Molecular Endocrinology, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, JapanInstitute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113-0032, JapanDepartment of Molecular Endocrinology, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, JapanPosttranslational modification (PTM) of proteins is used to regulate protein activity and stability. Histone PTMs are regarded as some of the most important, as they can directly regulate gene expression through chromatin reorganization. Recently, histone proteins were found to undergo succinylation, adding to other well-known PTMs such as acetylation, methylation, and phosphorylation. However, there is little information regarding the enzyme which catalyzes histone lysine succinylation. In fact, it is unclear whether this reaction is enzymatic. In this study, we tested histone succinylation activity in vitro using cell nuclear extracts of HepG2 cells. Although whole nuclear extracts did not show histone succinylation activity, we found that an SP 1.0 M KCl fraction of nuclear extracts indeed had such activity. These data offer the first direct evidence that histone succinylation is an enzymatic PTM as are other histone codes in the nucleus.http://dx.doi.org/10.1155/2017/8529404 |
| spellingShingle | Atsushi Yokoyama Shogo Katsura Akira Sugawara Biochemical Analysis of Histone Succinylation Biochemistry Research International |
| title | Biochemical Analysis of Histone Succinylation |
| title_full | Biochemical Analysis of Histone Succinylation |
| title_fullStr | Biochemical Analysis of Histone Succinylation |
| title_full_unstemmed | Biochemical Analysis of Histone Succinylation |
| title_short | Biochemical Analysis of Histone Succinylation |
| title_sort | biochemical analysis of histone succinylation |
| url | http://dx.doi.org/10.1155/2017/8529404 |
| work_keys_str_mv | AT atsushiyokoyama biochemicalanalysisofhistonesuccinylation AT shogokatsura biochemicalanalysisofhistonesuccinylation AT akirasugawara biochemicalanalysisofhistonesuccinylation |