Source:http://linkedlifedata.com/resource/pubmed/id/15607035
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2004-12-20
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pubmed:abstractText |
The hepatitis C virus is associated with the development of liver cirrhosis and hepatocellular carcinomas. Among the 10 polyproteins produced by the virus, no function has been clearly assigned to the non-structural 5A (NS5A) protein. This study was designed to identify the hepatocellular proteins that interact with NS5A of the HCV. Yeast two-hybrid experiments were performed with a human liver cDNA prey-library, using five different NS5A derivatives as baits, the full-length NS5A (NS5A-F, amino acid (aa) 1 approximately 447) and its four different derivatives, denoted as NS5A-A (aa 1 approximately 150), -B (aa 1 approximately 300), -C (aa 300 approximately 447) and D (aa 150 approximately 447). NS5A-F, NS5A-B and NS5A-C gave two, two and 10 candidate clones, respectively, including an AHNAK-related protein, the secreted frizzled-related protein 4 (SFRP4), the N-myc downstream regulated gene 1 (NDRG1), the cellular retinoic acid binding protein 1 (CRABP-1), ferritin heavy chain (FTH1), translokin, tumor-associated calcium signal transducer 2 (TACSTD2), phosphatidylinositol 4-kinase (PI4K) and centaurindelta 2 (CENTdelta2). However, NS5A-A produced no candidates and NS5A-D was not suitable as bait due to transcriptional activity. Based on an in vitro binding assay, CRABP-1, PI4K, CENTdelta2 and two unknown fusion proteins with maltose binding protein (MBP), were confirmed to interact with the glutathione S-transferase (GST)/NS5A fusion protein. Furthermore, the interactions of CRABP-1, PI4K and CENTdelta2 were not related to the PXXP motif (class II), as judged by a domain analysis. While their biological relevance is under investigation, the results contribute to a better understanding of the possible role of NS5A in hepatocellular signaling pathways.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1225-8687
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pubmed:author |
pubmed-author:AhnJiwonJ,
pubmed-author:ChaeSuhn-KeeSK,
pubmed-author:ChoiShin-JungSJ,
pubmed-author:ChungKyung-SookKS,
pubmed-author:HoeKwang-LaeKL,
pubmed-author:KimDong-UkDU,
pubmed-author:KimHyoung-ChinHC,
pubmed-author:KimKyung-ShinKS,
pubmed-author:LaneD MDM,
pubmed-author:NamMiyoungM,
pubmed-author:WonMisunM,
pubmed-author:YoonMichungM
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
741-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15607035-Hepacivirus,
pubmed-meshheading:15607035-Humans,
pubmed-meshheading:15607035-Liver,
pubmed-meshheading:15607035-Molecular Sequence Data,
pubmed-meshheading:15607035-Mutation,
pubmed-meshheading:15607035-Protein Binding,
pubmed-meshheading:15607035-Two-Hybrid System Techniques,
pubmed-meshheading:15607035-Viral Nonstructural Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus.
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pubmed:affiliation |
Korea Research Institute of Bioscience and Biotechnology (KRIBB), Yusong, Daejeon, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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