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Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain.

Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. Research Abstract Details 

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  • Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. Abstract Text:

    takashi kusakawaTakashi Kusakawa,tetsuro shimakamiTetsuro Shimakami,shuichi kanekoShuichi Kaneko,katsuji yoshiokaKatsuji Yoshioka,seishi murakamiSeishi Murakami,takashi kusakawaTakashi Kusakawa,tetsuro shimakamiTetsuro Shimakami,shuichi kanekoShuichi Kaneko,katsuji yoshiokaKatsuji Yoshioka,seishi murakamiSeishi Murakami,

    Hepatitis C Virus (HCV) non-structural proteins are major components of replication complex that is modulated by several host factors. We previously reported that nucleolin, a representative nucleolar marker, interacts with the NS5B through two separated sequences, amino acids (aa) 208-214 and 500-506, and that W208 in the former stretch is essential for both nucleolin-binding and HCV replication. Here we evaluated the role of the latter stretch aa 500-506 of WRHRARS in nucleolin-binding and HCV replication scanned by alanine-substituted clustered mutant (cm) or point mutant (pm). One tryptophan and three arginine residues in the sequence were found to be essential both for nucleolin-binding in vivo and HCV replication detected with a HCV subgenomic replicon transfected into Huh7 cells. NS5B-binding of nucleolin was further delineated by truncation and clustered mutants of nucleolin. Arginine-glycine-glycine (RGG) repeat in the Glycine arginine rich (GAR) domain were defined to be indispensable for NS5B-binding immunologically detected in in vivo and in vitro although short internal-truncations of RGG repeat are tolerable for NS5B-binding. These results indicate that nucleolin is a critical host factor for HCV replication through the direct interaction between W208 and several residues at the sequence, aa 500-505, of NS5B, and the long-turn motif including RGG repeat at nucleolin C-terminal.

    Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. Publishing Authors By Initials

    t kusakawaT Kusakawa,t shimakamiT Shimakami,s kanekoS Kaneko,k yoshiokaK Yoshioka,s murakamiS Murakami,t kusakawaT Kusakawa,t shimakamiT Shimakami,s kanekoS Kaneko,k yoshiokaK Yoshioka,s murakamiS Murakami,

    For similar proteins: viral proteins: viral nonstructural proteins research abstracts see: proteins: viral proteins: viral nonstructural proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 141

    Page Numbers: 917-27

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 27

    MONTH: Jun

    YEAR: 2007

    Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. Keywords Mesh Terms:

    KEYWORDS: Viral Nonstructural Proteins

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. Information

    Substance Name: Arginine

    Registry Number: 74-79-3

    Grant and Affiliation Information for Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain.

    AFFILIATION: Division of Signal Transduction, Cancer Research Institute, University Hospital, Kanazawa University, Takara-Machi, Kanazawa, Ishikawa, Japan.

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    GRANT:

    ACRONYM:

    MEDLINETA: J Biochem (Tokyo)

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