Histone deacetylase III interactions with BK polyomavirus large tumor antigen may affect protein stability

doi:10.1186/s12985-023-02128-6

CNU IR > College of Sustainable Environment and Recreation > Dept. of Sports Management > Periodical Articles > Item 310902800/34789

Please use this identifier to cite or link to this item: https://ir.cnu.edu.tw/handle/310902800/34789

Title:	Histone deacetylase III interactions with BK polyomavirus large tumor antigen may affect protein stability
Authors:	Hsu, Yueh-Han Chao, Chun-Nun Huang, Hsin-Yi Zhao, Pei-Wen Hsu, Pang-Hung Shen, Cheng-Huang Chen, San-Yuan Fang, Chiung-Yao
Contributors:	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
Keywords:	BKPyV Large T antigen Acetylation Protein stability HDAC3
Date:	2023
Issue Date:	2024-12-24 18:00:19 (UTC+8)
Publisher:	BMC
Abstract:	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.
Relation:	Virology Journal, v.20, n.1, Article 155
Appears in Collections:	[Dept. of Sports Management] Periodical Articles

Files in This Item:

File	Description	Size	Format
index.html		0Kb	HTML	13	View/Open
s12985-023-02128-6.pdf		1826Kb	Adobe PDF	7	View/Open

Loading...