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Biochemical Analysis of Histone Succinylation
Joint Authors
Sugawara, Akira
Yokoyama, Atsushi
Katsura, Shogo
Source
Biochemistry Research International
Issue
Vol. 2017, Issue 2017 (31 Dec. 2017), pp.1-7, 7 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2017-11-01
Country of Publication
Egypt
No. of Pages
7
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Yokoyama, Atsushi& Katsura, Shogo& Sugawara, Akira. 2017. Biochemical Analysis of Histone Succinylation. Biochemistry Research International،Vol. 2017, no. 2017, pp.1-7.
https://search.emarefa.net/detail/BIM-1139802
Modern Language Association (MLA)
Yokoyama, Atsushi…[et al.]. Biochemical Analysis of Histone Succinylation. Biochemistry Research International No. 2017 (2017), pp.1-7.
https://search.emarefa.net/detail/BIM-1139802
American Medical Association (AMA)
Yokoyama, Atsushi& Katsura, Shogo& Sugawara, Akira. Biochemical Analysis of Histone Succinylation. Biochemistry Research International. 2017. Vol. 2017, no. 2017, pp.1-7.
https://search.emarefa.net/detail/BIM-1139802
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1139802