Skip Navigation



Journal of Biochemistry Advance Access published online on January 3, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm037
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow Supplementary data
Right arrow All Versions of this Article:
141/2/269    most recent
mvm037v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Matsui, T.
Right arrow Articles by Maeda, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Matsui, T.
Right arrow Articles by Maeda, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society

RNA Recognition Mechanism of the Minimal Active Domain of the Human Immunodeficiency Virus Type-2 Nucleocapsid Protein

Takashi Matsui1, Yoshio Kodera1,*, Hiroshi Endoh1, Emi Miyauchi1, Hiroyoshi Komatsu2, Kazuki Sato3, Takeshi Tanaka4, Toshiyuki Kohno4 and Tadakazu Maeda1

1Department of Physics, School of Science, Kitasato University, Sagamihara, Kanagawa 228-8555, Japan
2Department of Immunology, School of Allied Health Sciences, Kitasato University, Sagamihara, Kanagawa 228-8555, Japan
3Department of Environmental Science, School of Human Environmental Science, Fukuoka Women's University, Higashi, Fukuoka 813-8529, Japan
4Mitsubishi Kagaku Institute of Life Sciences (MITILS), Machida, Tokyo 194-8511, Japan

*To whom correspondence should be addressed. Tel: +81-42-778-9540; Fax: +81-42-778-9541; E-mail: kodera{at}kitasato-u.ac.jp

Received October 14, 2006; Accepted December 10, 2006


  Abstract

NCp8 of HIV-2 contains two CCHC-type zinc fingers connected by a linker, and is involved in many critical steps of the virus life cycle. It was previously shown that the first zinc finger flanked by the linker is the minimal active domain for specific binding to viral RNA. In our previous study, we determined the three-dimensional structure of NCp8-f1, including the minimal active domain, and found that a hydrogen bond between Asn11 N{delta}H and Arg27 O stabilized the conformation of the linker in the vicinity of the zinc finger [Kodera et al. (1998) Biochemistry 37, 17704-17713]. In this study, RNA binding activities of NCp8-f1 and three types of its mutant peptides were analyzed by native PAGE assay. The activity and three-dimensional structure of NCp8-f1/N11A, in which alanine is substituted for Asn11 thereby affecting the conformation of the linker, was analyzed and compared with those of NCp8-f1. We demonstrated that the existence of Arg4 and/or Lys5 and Arg26 and/or Arg27 were necessary for binding RNA. Furthermore, the linker's flexible orientation, which is controlled by the hydrogen bond between Asn11 N{delta}H and Arg27 O, appears to be a structural basis for NCp8 existing as a multi-functional protein.

Key Words: HIV, nucleocapsid protein, NMR, RNA binding protein, zinc finger


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.