TY - JOUR
T1 - Biochemical analysis of histone succinylation
AU - Yokoyama, Atsushi
AU - Katsura, Shogo
AU - Sugawara, Akira
N1 - Funding Information:
The authors thank Dr. Shigeaki Kato (Iwaki Meisei University) for advice. This work was supported by Japan Society
Funding Information:
for the Promotion of Science (JSPS) (KAKENHI, Grants nos. 24658091 and 16K08606) (for Atsushi Yokoyama).
Publisher Copyright:
© 2017 Atsushi Yokoyama et al.
PY - 2017
Y1 - 2017
N2 - 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.
AB - 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.
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U2 - 10.1155/2017/8529404
DO - 10.1155/2017/8529404
M3 - Article
AN - SCOPUS:85042227457
VL - 2017
JO - Biochemistry Research International
JF - Biochemistry Research International
SN - 2090-2247
M1 - 8529404
ER -