TY - JOUR
T1 - Structural role of the secondary active domain of HIV-2 NCp8 in multi-functionality
AU - Matsui, Takashi
AU - Kodera, Yoshio
AU - Miyauchi, Emi
AU - Tanaka, Hidekazu
AU - Endoh, Hiroshi
AU - Komatsu, Hiroyoshi
AU - Tanaka, Takeshi
AU - Kohno, Toshiyuki
AU - Maeda, Tadakazu
N1 - Funding Information:
This study was supported in part by the Ministry of Education, Culture, Sports, Science, and Technology of Japan, by a grant from the National Project on Protein Structural and Function Analyses, and by Kitasato University Research Grants for Young Researchers. We thank Ms. Kuniko Kobayashi at the Mitsubishi Kagaku Institute of Life Sciences for helpful discussion.
PY - 2007/7/6
Y1 - 2007/7/6
N2 - Nucleocapsid protein of HIV, containing two CCHC-type zinc fingers connected by a linker, is a multi-functional protein involved in many critical steps of the HIV life cycle. Several in vitro investigations demonstrated that the reactivities of the first zinc finger flanked by the linker of HIV-1 NCp7 and HIV-2 NCp8 were essential for binding to viral RNA, however, that of the second zinc finger flanked by the linker of NCp7 was very weak and non-specific, whereas the part of NCp8 called NCp8-f2, interacted strongly and specifically with viral RNA. In this study, the three-dimensional structure of NCp8-f2 was determined for the first time. Furthermore, we established that NCp8-f2 specifically binds to the stem-loop SD in viral RNA, and that the hydrophobic cleft and the basic residues close to the cleft were essential for specific binding to SD. We discuss the functional significance of NCp8-f2 for NCp8 being a multi-functional protein.
AB - Nucleocapsid protein of HIV, containing two CCHC-type zinc fingers connected by a linker, is a multi-functional protein involved in many critical steps of the HIV life cycle. Several in vitro investigations demonstrated that the reactivities of the first zinc finger flanked by the linker of HIV-1 NCp7 and HIV-2 NCp8 were essential for binding to viral RNA, however, that of the second zinc finger flanked by the linker of NCp7 was very weak and non-specific, whereas the part of NCp8 called NCp8-f2, interacted strongly and specifically with viral RNA. In this study, the three-dimensional structure of NCp8-f2 was determined for the first time. Furthermore, we established that NCp8-f2 specifically binds to the stem-loop SD in viral RNA, and that the hydrophobic cleft and the basic residues close to the cleft were essential for specific binding to SD. We discuss the functional significance of NCp8-f2 for NCp8 being a multi-functional protein.
KW - 2D NMR
KW - HIV
KW - Nucleocapsid protein
KW - RNA binding protein
KW - Zinc finger
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U2 - 10.1016/j.bbrc.2007.04.141
DO - 10.1016/j.bbrc.2007.04.141
M3 - Article
C2 - 17511966
AN - SCOPUS:34249031153
VL - 358
SP - 673
EP - 678
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -
