Eukaryotic translation initiation factor 5A-1 is a
protein that in humans is encoded by the EIF5Agene.[5]
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
polyaminespermidine 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]
Faundes-Banka syndrome
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. It was named after Víctor Faundes and Siddharth Banka.
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
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^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.
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^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.
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10.1002/wrna.1211.
PMID24402910.
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Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J (December 1992). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–969.
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PMID1286667.
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Chung SI, Park MH, Folk JE, Lewis MS (February 1991). "Eukaryotic initiation factor 5A: the molecular form of the hypusine-containing protein from human erythrocytes". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1076 (3): 448–451.
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PMID1900436.
Koettnitz K, Kappel B, Baumruker T, Hauber J, Bevec D (July 1994). "The genomic structure encoding human initiation factor eIF-5A". Gene. 144 (2): 249–252.
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Klier H, Csonga R, Joäo HC, Eckerskorn C, Auer M, Lottspeich F, Eder J (November 1995). "Isolation and structural characterization of different isoforms of the hypusine-containing protein eIF-5A from HeLa cells". Biochemistry. 34 (45): 14693–14702.
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10.1021/bi00045a010.
PMID7578077.
Koettnitz K, Wöhl T, Kappel B, Lottspeich F, Hauber J, Bevec D (July 1995). "Identification of a new member of the human eIF-5A gene family". Gene. 159 (2): 283–284.
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Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174.
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Liu YP, Nemeroff M, Yan YP, Chen KY (1997). "Interaction of eukaryotic initiation factor 5A with the human immunodeficiency virus type 1 Rev response element RNA and U6 snRNA requires deoxyhypusine or hypusine modification". Biological Signals. 6 (3): 166–174.
doi:
10.1159/000109123.
PMID9285100.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156.
doi:
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PMID9373149.