PUBLICATION
Characterization of dFMR1, a Drosophila melanogaster homolog of the fragile X mental retardation protein
- Authors
- Wan, L., Dockendorff, T.C., Jongens, T.A., and Dreyfuss, G.
- ID
- ZDB-PUB-020806-1
- Date
- 2000
- Source
- Molecular and cellular biology 20(22): 8536-8547 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Motifs
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Antibodies, Monoclonal
- Apoptosis/genetics
- Cloning, Molecular
- Drosophila melanogaster/embryology
- Drosophila melanogaster/genetics*
- Embryo, Nonmammalian
- Fragile X Mental Retardation Protein
- Gene Expression Regulation, Developmental
- Genes, Dominant
- Insect Proteins/genetics*
- Insect Proteins/immunology
- Insect Proteins/metabolism*
- Molecular Sequence Data
- Nerve Tissue Proteins/genetics*
- Nerve Tissue Proteins/immunology
- Nerve Tissue Proteins/metabolism
- RNA/metabolism
- RNA-Binding Proteins*
- Sequence Homology, Amino Acid
- PubMed
- 11046149 Full text @ Mol. Cell. Biol.
Citation
Wan, L., Dockendorff, T.C., Jongens, T.A., and Dreyfuss, G. (2000) Characterization of dFMR1, a Drosophila melanogaster homolog of the fragile X mental retardation protein. Molecular and cellular biology. 20(22):8536-8547.
Abstract
Fragile X syndrome is the most common inherited form of mental retardation. It is caused by loss of FMR1 gene activity due to either lack of expression or expression of a mutant form of the protein. In mammals, FMR1 is a member of a small protein family that consists of FMR1, FXR1, and FXR2. All three members bind RNA and contain sequence motifs that are commonly found in RNA-binding proteins, including two KH domains and an RGG box. The FMR1/FXR proteins also contain a 60S ribosomal subunit interaction domain and a protein-protein interaction domain which mediates homomer and heteromer formation with each family member. Nevertheless, the specific molecular functions of FMR1/FXR proteins are unknown. Here we report the cloning and characterization of a Drosophila melanogaster homolog of the mammalian FMR1/FXR gene family. This first invertebrate homolog, termed dfmr1, has a high degree of amino acid sequence identity/similarity with the defined functional domains of the FMR1/FXR proteins. The dfmr1 product binds RNA and is similar in subcellular localization and embryonic expression pattern to the mammalian FMR1/FXR proteins. Overexpression of dfmr1 driven by the UAS-GAL4 system leads to apoptotic cell loss in all adult Drosophila tissues examined. This phenotype is dependent on the activity of the KH domains. The ability to induce a dominant phenotype by overexpressing dfmr1 opens the possibility of using genetic approaches in Drosophila to identify the pathways in which the FMR1/FXR proteins function.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping