The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

EIF1AX  -  eukaryotic translation initiation factor...

Homo sapiens

Synonyms: EIF1A, EIF1AP1, EIF4C, Eukaryotic translation initiation factor 1A, X-chromosomal, Eukaryotic translation initiation factor 4C, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of EIF1AX

  • Here, we assess the use of IF1/eIF1A and IF2/eIF5B in universal and partial phylogenetic studies by comparison of sequence information from species within all three phylogenetic domains and among closely related strains of Haemophilus parainfluenzae [1].
  • Overexpression of the human eIF-1A cDNA in Escherichia coli and subsequent purification enabled us to prepare large quantities of active factor [2].

High impact information on EIF1AX

  • The 40S subunit in 48S complexes formed at the initiation codon of mRNA is bound to eukaryotic initiation factor (eIF) 3, eIF1, eIF1A, and an eIF2/GTP/Met-tRNAi(Met) ternary complex and can therefore not join a 60S subunit directly to form an 80S ribosome [3].
  • The assembly defects of the OB-fold mutation can be attributed to reduced 40S-binding of eIF1A, whereas deltaC impairs eIF1A function on the ribosome [4].
  • Truncating the C-terminus (deltaC) or mutating OB-fold residues (66-70) of eIF1A reduced general translation in vivo but increased GCN4 translation (Gcd- phenotype) in a manner suppressed by overexpressing TC [4].
  • Unexpectedly, Imp13 also shows export activity towards the translation initiation factor eIF1A and is thus a case where a single importin beta-like receptor transports different substrates in opposite directions [5].
  • We demonstrate herein that (i) the "analogous" translation initiation factors IF-1 and eIF-1A are actually related in sequence, (ii) the "eukaryotic" translation factor SUI1 is universal in distribution, and (iii) the eukaryotic/archaeal translation factor eIF-5A is homologous to the bacterial translation factor EF-P [6].

Biological context of EIF1AX

  • The protein amino acid sequence of wheat germ eIF-4C is 68% identical with the mammalian protein, and, allowing for the most conservative substitutions, the proteins are 76% similar [7].
  • IF1/eIF1A and IF2/eIF5B, two conserved translation initiation factors are involved in this important step of protein biosynthesis [1].
  • Disruption of either isoleucine residue in the eIF1A C-terminal sequence DIDDI reduces the rate constant for GTP hydrolysis by approximately 20-fold, whereas changing the aspartic acid residues has no effect [8].
  • To better elucidate its precise role in promoting the translation initiation process, the yeast form of eIF1A has been identified in Saccharomyces cerevisiae and purified to homogeneity on the basis of its cross-reaction with antibodies prepared against mammalian eIF1A [9].
  • Deletion/disruption of TIF11 demonstrates that eIF1A is essential for cell growth [9].

Anatomical context of EIF1AX


Associations of EIF1AX with chemical compounds

  • From the chemical sequencing of the rabbit protein, it was noted that at least two different eIF-4C molecules were present which differed by conservative substitutions at three positions (2 aspartic acid for glutamic acid switches and 1 valine for isoleucine switch) [7].

Other interactions of EIF1AX

  • Here, we have identified the binding interface between human eIF1A and the C-terminal domain of eIF5B by using solution NMR [10].
  • Here, we report the quantitative characterization of energetic interactions between eIF1A, eIF5 and the AUG codon in an in vitro reconstituted yeast translation initiation system [12].
  • In addition, eIF1A, eIF4F (or the C-terminal fragment of eIF4G), and eIF4A strongly stimulated the assembly of this complex, whereas eIF4B had no effect [13].

Analytical, diagnostic and therapeutic context of EIF1AX

  • NMR titration experiments showed that eIF1A binds single-stranded RNA oligonucleotides in a site-specific, but non-sequence-specific manner, hinting at an mRNA interaction rather than specific rRNA or tRNA binding [14].
  • The RA for eIF1A was higher (P </= 0.05) in 8- to 16-cell embryos derived from cows than those from the control group [11].


  1. Remarkable conservation of translation initiation factors: IF1/eIF1A and IF2/eIF5B are universally distributed phylogenetic markers. Sørensen, H.P., Hedegaard, J., Sperling-Petersen, H.U., Mortensen, K.K. IUBMB Life (2001) [Pubmed]
  2. Protein synthesis initiation factor eIF-1A is a moderately abundant RNA-binding protein. Wei, C.L., MacMillan, S.E., Hershey, J.W. J. Biol. Chem. (1995) [Pubmed]
  3. Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Unbehaun, A., Borukhov, S.I., Hellen, C.U., Pestova, T.V. Genes Dev. (2004) [Pubmed]
  4. The eIF1A C-terminal domain promotes initiation complex assembly, scanning and AUG selection in vivo. Fekete, C.A., Applefield, D.J., Blakely, S.A., Shirokikh, N., Pestova, T., Lorsch, J.R., Hinnebusch, A.G. EMBO J. (2005) [Pubmed]
  5. Importin 13: a novel mediator of nuclear import and export. Mingot, J.M., Kostka, S., Kraft, R., Hartmann, E., Görlich, D. EMBO J. (2001) [Pubmed]
  6. Universally conserved translation initiation factors. Kyrpides, N.C., Woese, C.R. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. Determination of the amino acid sequence of rabbit, human, and wheat germ protein synthesis factor eIF-4C by cloning and chemical sequencing. Dever, T.E., Wei, C.L., Benkowski, L.A., Browning, K., Merrick, W.C., Hershey, J.W. J. Biol. Chem. (1994) [Pubmed]
  8. Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining. Acker, M.G., Shin, B.S., Dever, T.E., Lorsch, J.R. J. Biol. Chem. (2006) [Pubmed]
  9. Characterization of yeast translation initiation factor 1A and cloning of its essential gene. Wei, C.L., Kainuma, M., Hershey, J.W. J. Biol. Chem. (1995) [Pubmed]
  10. Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: a new interaction between old partners. Marintchev, A., Kolupaeva, V.G., Pestova, T.V., Wagner, G. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  11. Improvement of the developmental capacity of oocytes from prepubertal cattle by intraovarian insulin-like growth factor-I application. Oropeza, A., Wrenzycki, C., Herrmann, D., Hadeler, K.G., Niemann, H. Biol. Reprod. (2004) [Pubmed]
  12. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. Maag, D., Algire, M.A., Lorsch, J.R. J. Mol. Biol. (2006) [Pubmed]
  13. A cross-kingdom internal ribosome entry site reveals a simplified mode of internal ribosome entry. Terenin, I.M., Dmitriev, S.E., Andreev, D.E., Royall, E., Belsham, G.J., Roberts, L.O., Shatsky, I.N. Mol. Cell. Biol. (2005) [Pubmed]
  14. The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Battiste, J.L., Pestova, T.V., Hellen, C.U., Wagner, G. Mol. Cell (2000) [Pubmed]
WikiGenes - Universities