Crystal structure of zinc-finger domain of Nanos and its functional implications.
Nanos is an RNA-binding protein that is involved in the development and maintenance of germ cells. In combination with Pumilio, Nanos binds to the 3' untranslated region of a messenger RNA and represses its translation. Nanos has two conserved Cys-Cys-His-Cys zinc-finger motifs that are indispensable for its function. In this study, we have determined the crystal structure of the zinc-finger domain of zebrafish Nanos, for the first time revealing that Nanos adopts a novel zinc-finger structure. In addition, Nanos has a conserved basic surface that is directly involved in RNA binding. Our results provide the structural basis for further studies to clarify Nanos function.
Hashimoto
Hiroshi
H
Graduate School of Nanobioscience, Yokohama City University, Tsurumi-ku, Yokohama, Kanagawa, Japan. hash@tsurumi.yokohama-cu.ac.jp
Hara
Kodai
K
Hishiki
Asami
A
Kawaguchi
Shigeta
S
Shichijo
Naoki
N
Nakamura
Keishi
K
Unzai
Satoru
S
Tamaru
Yutaka
Y
Shimizu
Toshiyuki
T
Sato
Mamoru
M
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D013329:Structure-Activity Relationship; D015027:Zebrafish / Q000378:metabolism*; D029961:Zebrafish Proteins / Q000737:chemistry* / Q000378:metabolism*; D016335:Zinc Fingers
D016601:RNA-Binding Proteins; D029961:Zebrafish Proteins; C440015:nanos3 protein, zebrafish; D012313:RNA