Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/34789
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    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

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