Characterization of PRMT associated with the NS3 of hepatitis C virus = 간염 C형 바이러스의 NS3 단백질과 결합하는 PRMT의 특성에 관한 연구

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The Hepatitis C virus (HCV) is a major inducer of chronic hepatitis, and its chronic infection is associated with liver cirrhosis, and eventually, development of hepatocellular carcinoma. To develop therapeutic tools against of hepatocellular carcinoma caused by chronic infection of HCV, it is important to understand molecular mechanism by which HCV causes liver pathogenesis and which cellular genes are involved in hepatocellular carcinogenesis. A number of studies suggest that the core protein of HCV is a major viral factor in in hepatocellular carcinogenesis. Also, NS3 protein of HCV has been shown to be implicated in the liver pathogenesis. To search for cellular targets of the NS3 protein, we conducted a yeast two-hybrid screen. We found that Janus kinase-binding protein 1 (JBP1), known as a human homologue of Shk1 kinase-binding protein 1 of the fission yeast (Skb1Hs), interacts with the nonstructural protein 3 of the hepatitis C virus by a yeast two-hybrid screen. Amino acid sequence analysis revealed that Skb1Hs/JBP1 contains conserved motifs of S-adenosylmethionine-dependent protein arginine methyltransferases (PRMTs). Here, we demonstrate that Skb1Hs/JBP1, named PRMT5, is a distinct member of the protein arginine methyltransferase family. Recombinant PRMT5 protein purified from human cells methylates myelin basic protein and histone. Myelin basic protein methylated by PRMT5 contains monomethylated and dimethylated arginine residues. Sedimentation analysis of the purified PRMT5 on a sucrose density gradient indicates that PRMT5 forms distinct homo-oligomeric complexes, including dimer and tetramer, which comigrate with the enzyme activity. Western blot analysis of sedimentation fractions suggests that endogenous PRMT5 is present as a homo-oligomer in a 293T cell extract. This finding prompted us to examine the possibility of whether arginine residues of the NS3 protein are methylated by protein arginine methyltransferases (PRMTs). PRMTs transfer the me...
Advisors
Choe, Joon-Horesearcher최준호researcher
Description
한국과학기술원 : 생물과학과,
Publisher
한국과학기술원
Issue Date
2002
Identifier
174551/325007 / 000985382
Language
eng
Description

학위논문(박사) - 한국과학기술원 : 생물과학과, 2002.2, [ v, 108 p. ]

Keywords

NS3; PRMT; 간염바이러스; NS3; Hepatitis C virus

URI
http://hdl.handle.net/10203/27522
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=174551&flag=dissertation
Appears in Collection
BS-Theses_Ph.D.(박사논문)
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