PUBLICATION
Purification, crystallization and initial X-ray diffraction study of the zinc-finger domain of zebrafish Nanos
- Authors
- Hashimoto, H., Kawaguchi, S., Hara, K., Nakamura, K., Shimizu, T., Tamaru, Y., and Sato, M.
- ID
- ZDB-PUB-090914-21
- Date
- 2009
- Source
- Acta crystallographica. Section F, Structural biology and crystallization communications 65(Pt 9): 959-961 (Journal)
- Registered Authors
- Tamaru, Yutaka
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Crystallization
- Crystallography, X-Ray
- Electrophoresis, Polyacrylamide Gel
- Molecular Sequence Data
- RNA-Binding Proteins
- Sequence Alignment
- X-Ray Diffraction*
- Zebrafish/metabolism*
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/isolation & purification*
- Zinc Fingers*
- PubMed
- 19724144 Full text @ Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Citation
Hashimoto, H., Kawaguchi, S., Hara, K., Nakamura, K., Shimizu, T., Tamaru, Y., and Sato, M. (2009) Purification, crystallization and initial X-ray diffraction study of the zinc-finger domain of zebrafish Nanos. Acta crystallographica. Section F, Structural biology and crystallization communications. 65(Pt 9):959-961.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping