High impact information on qkr58E-1

• Further studies revealed that the 8.5-kb transcript arises from the fusion of EIF4EBP3 with the mammalian homologue of Drosophila MASK (multiple ankyrin repeats, single KH domain), which is crucial for photoreceptor differentiation, cell survival, and proliferation [1].
• To identify GSG domain family members, we searched data bases for expressed sequence tags encoding related portions of the Sam68 KH domain [2].
• 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 [3].
• Nucleotide sequence analysis of cDNA clones revealed a high degree of similarity to vertebrate RNA binding KH domain proteins, suggesting a function of the MUB protein in binding and stabilizing of specific mRNAs in the mushroom bodies [4].
• However, a single missense mutation (I304N) in the second KH domain of FMRP gives rise to a particularly severe case of Fragile X syndrome [5].

Biological context of qkr58E-1

• We find that these KH domain mutations result in partial loss of function or no significant loss of function for the phenotypes assayed [3].
• Here we show that the I307N point mutation does not completely unfold the KH domain [5].
• In addition, the Arabidopsis genome contains 26 KH domain proteins [6].

References