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.
Graduate School of Nanobioscience, Yokohama City University, Tsurumi-ku, Yokohama, Kanagawa, Japan. hash@tsurumi.yokohama-cu.ac.jp
Hiroshi
H
Hashimoto
Kodai
K
Hara
Asami
A
Hishiki
Shigeta
S
Kawaguchi
Naoki
N
Shichijo
Keishi
K
Nakamura
Satoru
S
Unzai
Yutaka
Y
Tamaru
Toshiyuki
T
Shimizu
Mamoru
M
Sato
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