PUBLICATION
Crystal structure of zinc-finger domain of Nanos and its functional implications
- Authors
- Hashimoto, H., Hara, K., Hishiki, A., Kawaguchi, S., Shichijo, N., Nakamura, K., Unzai, S., Tamaru, Y., Shimizu, T., and Sato, M.
- ID
- ZDB-PUB-101018-32
- Date
- 2010
- Source
- EMBO reports 11(11): 848-853 (Journal)
- Registered Authors
- Tamaru, Yutaka
- Keywords
- crystal structure, germ cell, Nanos, RNA-binding protein, translational regulation
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Crystallography, X-Ray
- Models, Molecular
- Molecular Sequence Data
- Protein Binding
- Protein Structure, Tertiary
- RNA/metabolism
- RNA-Binding Proteins
- Sequence Alignment
- Structural Homology, Protein
- Structure-Activity Relationship
- Zebrafish/metabolism*
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/metabolism*
- Zinc Fingers*
- PubMed
- 20948543 Full text @ EMBO Rep.
Citation
Hashimoto, H., Hara, K., Hishiki, A., Kawaguchi, S., Shichijo, N., Nakamura, K., Unzai, S., Tamaru, Y., Shimizu, T., and Sato, M. (2010) Crystal structure of zinc-finger domain of Nanos and its functional implications. EMBO reports. 11(11):848-853.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping