Purification, crystallization and initial X-ray diffraction study of the zinc-finger domain of zebrafish Nanos.
Nanos is a highly conserved RNA-binding protein in higher eukaryotes and acts as a key regulator protein involved in translational control utilizing the 3' untranslated region of mRNA. The C-terminal domain of Nanos has two conserved and novel CCHC-type zinc-finger motifs that are responsible for the function of Nanos. To clarify the structural basis of the function of Nanos, the C-terminal domain (residues 59-159) of zebrafish Nanos was overexpressed, purified and crystallized. The crystal belonged to space group P6(3), with unit-cell parameters a = b = 100.9, c = 71.5 A, gamma = 120 degrees. Structure determination by the MAD/SAD method is now in progress.
Hashimoto
Hiroshi
H
Graduate School of Nanobioscience, Yokohama City University, Tsurumi, Yokohama, Kanagawa, Japan. hash@tsurumi.yokohama-cu.ac.jp
Kawaguchi
Shigeta
S
Hara
Kodai
K
Nakamura
Keishi
K
Shimizu
Toshiyuki
T
Tamaru
Yutaka
Y
Sato
Mamoru
M
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D016601:RNA-Binding Proteins; D016415:Sequence Alignment; D014961:X-Ray Diffraction; D015027:Zebrafish / Q000378:metabolism*; D029961:Zebrafish Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D016335:Zinc Fingers
D016601:RNA-Binding Proteins; D029961:Zebrafish Proteins; C440015:nanos3 protein, zebrafish