資料載入中.....
|
請使用永久網址來引用或連結此文件:
https://ir.cnu.edu.tw/handle/310902800/34789
|
| 標題: | Histone deacetylase III interactions with BK polyomavirus large tumor antigen may affect protein stability |
| 作者: | Hsu, Yueh-Han
Chao, Chun-Nun
Huang, Hsin-Yi
Zhao, Pei-Wen
Hsu, Pang-Hung
Shen, Cheng-Huang
Chen, San-Yuan
Fang, Chiung-Yao |
| 貢獻者: | Chia Yi Christian Hosp, Ditmanson Med Fdn, Dept Internal Med, Div Nephrol
Min Hwei Jr Coll Hlth Care Management, Dept Nursing
Chia Yi Christian Hosp, Ditmanson Med Fdn, Dept Pediat
Natl Chung Cheng Univ, Dept Biomed Sci
Asia Univ, Dept Med Lab Sci & Biotechnol
Chia Yi Christian Hosp, Ditmanson Med Fdn, Dept Med Res
Natl Taiwan Ocean Univ, Dept Biosci & Biotechnol
Chiayi Christian Hosp, Ditmanson Med Fdn, Dept Urol
Chia Yi Christian Hosp, Ditmanson Med Fdn, Dept Chinese Med
Chia Nan Univ Pharm & Sci, Dept Sports Management |
| 關鍵字: | BKPyV
Large T antigen
Acetylation
Protein stability
HDAC3 |
| 日期: | 2023 |
| 上傳時間: | 2024-12-24 18:00:19 (UTC+8) |
| 出版者: | BMC |
| 摘要: | BackgroundHuman polyomavirus BK (BKPyV) causes associated nephropathy and contributes to urinary tract cancer development in renal transplant recipients. Large tumor antigen (LT) is an early protein essential in the polyomavirus life cycle. Protein acetylation plays a critical role in regulating protein stability, so this study investigated the acetylation of the BKPyV LT protein.MethodsThe BKPyV LT nucleotide was synthesized, and the protein was expressed by transfection into permissive cells. The BKPyV LT protein was immunoprecipitated and subjected to LC-MS/MS analysis to determine the acetylation residues. The relative lysine was then mutated to arginine in the LT nucleotide and BKPyV genome to analyze the role of LT lysine acetylation in the BKPyV life cycle.ResultsBKPyV LT acetylation sites were identified at Lys3 and Lys230 by mass spectrometry. HDAC3 and HDAC8 and their deacetylation activity are required for BKPyV LT expression. In addition, mutations of Lys3 and Lys230 to arginine increased LT expression, and the interaction of HDAC3 and LT was confirmed by coimmunoprecipitation.ConclusionsHDAC3 is a newly identified protein that interacts with BKPyV LT, and LT acetylation plays a vital role in the BKPyV life cycle. |
| 關聯: | Virology Journal, v.20, n.1, Article 155 |
| 顯示於類別: | [運動管理系] 期刊論文
|
文件中的檔案:
| 檔案 |
描述 |
大小 | 格式 | 瀏覽次數 |
|---|
| index.html | | 0Kb | HTML | 12 | 檢視/開啟 | | s12985-023-02128-6.pdf | | 1826Kb | Adobe PDF | 5 | 檢視/開啟 |
|
在CNU IR中所有的資料項目都受到原著作權保護.
|
