Journal
GENETICS
Volume 175, Issue 3, Pages 1241-1250Publisher
GENETICS SOCIETY AMERICA
DOI: 10.1534/genetics.106.068908
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Funding
- NIGMS NIH HHS [GM068468, R15 GM068468] Funding Source: Medline
- NIMH NIH HHS [MH067622-01, R01 MH066197, MH66197, R15 MH067622] Funding Source: Medline
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Fragile X mental retardation proteins (FMRP) are RNA-binding proteins that interact with a subset of cellular RNAs. Several RNA-binding domains have been identified in FMRP, but the contribution of these individual domains to FMRP function in an animal model is not well understood. In this study, we have generated flies with point Mutations in the KH domains of the Drosophila melanogaster fragile X gene (dfmr1) in the context of a genomic rescue fragment. The substitutions of conserved isoleucine residues within the KH domains with asparagine are thought to impair binding of RNA substrates and perhaps the ability of FMRP to assemble into mRNP complexes. The Mutants were analyzed for defects in development and behavior that are associated with deletion null alleles of dfmr1. We find that these KH domain mutations result in partial loss of function or no significant loss of function for the phenotypes assayed. The phenotypes resulting from these KH domain mutants imply that the capacities of the mutant proteins to bind RNA and form functional mRNP complexes are not wholly disrupted and are consistent with biochemical models suggesting that RNA-binding domains of FMRP can function independently.
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