Disease relevance of eIF-4a

• Among these proteins are eIF-4A, an essential component of the cap-binding complex, numerous yeast proteins required for pre-mRNA splicing, and proteins from yeast and E. coli necessary for ribosome assembly [1].

High impact information on eIF-4a

• This polar granule component shows significant sequence similarity to eIF-4A, a translation initiation factor that binds to mRNA, and to other helicases [2].
• The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A [3].
• The predicted amino acid sequence is very similar to those of the translation initiation factor eIF-4A and the human nuclear antigen p68 [3].
• We show that Su(dpp)(YE9) maps to eIF4A and that this allele is associated with a substitution, arginine 321 to histidine, at a well-conserved amino acid and behaves genetically as a dominant-negative mutation [4].
• No expression was detected of the eIF4A-related gene CG7483 [5].

Biological context of eIF-4a

• The two mRNAs contain the same open reading frame and produce the identical eIF4A protein [5].
• We observed ubiquitous expression of eIF4A mRNA and protein during Drosophila embryogenesis [5].
• A combination of immunoblotting and labelling with [(35)S]methionine + [(35)S]cysteine revealed the existence of a single eIF4A isoform encoded by a previously reported gene that maps to chromosome 2L at 26A7-9 [5].

Other interactions of eIF-4a

• Yeast two-hybrid analysis demonstrated the in vivo interaction of Drosophila eIF4G with the N-terminal third of eIF4A [5].

Analytical, diagnostic and therapeutic context of eIF-4a

• Two-dimensional gel electrophoresis and microsequencing allowed us to purify eIF4A, and generate specific polyclonal antibodies [5].

References