Disease relevance of Eif5b

• For structural and functional investigations of the factor, we have raised and characterised monoclonal antibodies against E. coli IF2 [1].

High impact information on Eif5b

• DNA transfection experiments of NIH 3T3 fibroblasts using an alpha 1(I) promoter-CAT chimeric gene in which mutations were introduced that either improved or decreased the binding affinity of IF-2 for its recognition site, strongly suggest that IF-2 acts as a transcriptional inhibitor of the mouse alpha 1(I) collagen gene [2].
• IF-2 was purified to homogeneity from mouse lymphocyte nuclear extracts by ion-exchange chromatography and two different steps of DNA affinity chromatography, one using the wild-type IF-2-binding site as affinity ligand and one using a mutated IF-2-binding site that has a higher affinity for the factor [2].
• A mutation in the proximal IF1 binding site increases promoter activity 4-fold, a mutation in the IF2 binding site increases this activity 10-fold and a mutation in the CBF binding site decreases this activity 4-5-fold [3].
• We propose that mutually competitive binding of IF2 and CBF could play a role in the control of the alpha 1(I) collagen promoter [3].
• We have isolated and characterised a recombinant plasmid containing cDNA copies of the IF2 mutant mRNA [4].

Biological context of Eif5b

• By using the established amino acid sequence of the IF2 H-chain and a knowledge of the genetic code, 14 oligonucleotides were assigned within the constant region and four within the variable region of the IF2 H-chain [5].

Anatomical context of Eif5b

• A mutant cell line (IF2) derived from the mouse myeloma MOPC 21 has been used for the isolation and sequence analysis of H-chain mRNA [5].

References