EIF5A

EIF5A

EIF5A

Protein-coding gene in humans

Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene.[5]

Quick Facts Available structures, PDB ...

It is the only known protein to contain the unusual amino acid hypusine [Nε-(4-amino-2-hydroxybutyl)-lysine], which is synthesized on eIF5A at a specific lysine residue from the polyamine spermidine by two catalytic steps.[6]

EF-P is the bacterial homolog of eIF5A, which is modified post-translationally in a similar but distinct way.[7][8] Both proteins are believed to catalyze peptide bond formation and help resolve ribosomal stalls, making them elongation factors despite the "initiation factor" name originally assigned.[9]

Clinical relevance

Germline deleterious heterozygous EIF5A variants cause Faundes-Banka syndrome.[10][11] This rare human disorder is characterized by variable combinations of developmental delay, microcephaly, micrognathia and dysmorphic features.

References

  1. [1]
    ENSG00000288145 GRCh38: Ensembl release 89: ENSG00000132507, ENSG00000288145 – Ensembl, May 2017
  2. [2]
    GRCm38: Ensembl release 89: ENSMUSG00000078812 – Ensembl, May 2017
  3. [3]
    "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. [4]
    "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. [5]
    Steinkasserer A, Jones T, Sheer D, Koettnitz K, Hauber J, Bevec D (February 1995). "The eukaryotic cofactor for the human immunodeficiency virus type 1 (HIV-1) rev protein, eIF-5A, maps to chromosome 17p12-p13: three eIF-5A pseudogenes map to 10q23.3, 17q25, and 19q13.2". Genomics. 25 (3): 749–752. doi:10.1016/0888-7543(95)80025-H. PMID 7759117.
  6. [6]
    Wolff EC, Kang KR, Kim YS, Park MH (August 2007). "Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification". Amino Acids. 33 (2): 341–350. doi:10.1007/s00726-007-0525-0. PMC 2572820. PMID 17476569.
  7. [7]
    Park JH, Johansson HE, Aoki H, Huang BX, Kim HY, Ganoza MC, Park MH (January 2012). "Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)". The Journal of Biological Chemistry. 287 (4): 2579–2590. doi:10.1074/jbc.M111.309633. PMC 3268417. PMID 22128152.
  8. [8]
    Peil L, Starosta AL, Virumäe K, Atkinson GC, Tenson T, Remme J, Wilson DN (August 2012). "Lys34 of translation elongation factor EF-P is hydroxylated by YfcM". Nature Chemical Biology. 8 (8): 695–697. doi:10.1038/nchembio.1001. PMID 22706199.
  9. [9]
    Rossi D, Kuroshu R, Zanelli CF, Valentini SR (2013). "eIF5A and EF-P: two unique translation factors are now traveling the same road". Wiley Interdisciplinary Reviews. RNA. 5 (2): 209–222. doi:10.1002/wrna.1211. PMID 24402910. S2CID 25447826.
  10. [10]
    Faundes V, Jennings MD, Crilly S, Legraie S, Withers SE, Cuvertino S, Davies SJ, Douglas AG, Fry AE, Harrison V, Amiel J, Lehalle D, Newman WG, Newkirk P, Ranells J, Splitt M, Cross LA, Saunders CJ, Sullivan BR, Granadillo JL, Gordon CT, Kasher PR, Pavitt GD, Banka S (February 2021). "Impaired eIF5A function causes a Mendelian disorder that is partially rescued in model systems by spermidine". Nature Communications. 12 (1): 833. Bibcode:2021NatCo..12..833F. doi:10.1038/s41467-021-21053-2. PMC 7864902. PMID 33547280.
  11. [11]
    "OMIM Entry - # 619376 - FAUNDES-BANKA SYNDROME; FABAS". omim.org. Retrieved 2022-01-03.

Further reading

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