Hypusine Formation on Eukaryotic Initiation Factor 5A: Biochemistry and Function (Biological Signals Ser. Series, 3) - kelloggchurch.org

EIF5A - Wikipedia.

Eukaryotic initiation factor 5A eIF-5A is the only protein in nature that contains hypusine, an unusual amino acid formed post-translationally by deoxyhypusine synthase and deoxyhypusine hydroxylase. Genetic and pharmacological evidence suggests that eIF-5A is essential for cell survival and proliferation. Jan 01, 2003 · Received October 4, 2002; accepted October 25, 2002. Eukaryotic initiation factor 5A eIF-5A, ubiquitous in both eukaryotes and archaebacteria, consists of about 140 amino acid residues and was initially named based on the findings that eIF-5A could be isolated from the ribosome-bound fraction and stimulate the synthesis of methionyl-puromycin 1, 2. Dec 01, 1993 · M. H. Park, E. C. Wolff and J. E. Folk Hypusine [NE-4amino-2-hydroxybutyl-L-lysine] is a most remarkable amino acid, occurring in all eukaryotic cells, yet occupying only a single position in one protein, eukaryotic protein synthesis initiation factor 5A eIF 5A. The natural amino acid hypusine Nϵ -4-amino-2-hydroxybutyl lysine is derived from the polyamine spermidine, and occurs only in a single family of cellular proteins, eukaryotic translation factor 5A eIF5A isoforms. Hypusine is formed by conjugation of the aminobutyl moiety of spermidine to a specific lysine residue of this protein. Eukaryotic translation initiation factor 5A eIF5A is found in all eukaryotes and archaebacteria and is unique in that it is the only protein known to undergo a two‐step post‐translational modification of a highly conserved lysine residue to form hypusine [[1, 2]].First, a spermidine moiety is conjugated to the epsilon amino group of the lysine, catalysed by deoxyhypusine synthase DHS.

By considering the best alignments found i.e. an E value better than 10 –6, the human eIF-5A sequence is significantly similar to many proteins defined as `initiation factor 5A', thus confirming that this protein is well conserved within different organisms, in both eukaryotic sequences 1–35 and archea sequences 36–48 groups. hypusine formation on the 18 kDa protein in cytosolic lysates derived from NB-15. Biochemistry and function of hypusine formation on. eukaryotic initiation factor 5A. Biol. Oct 12, 2012 · Cell proliferation is tightly controlled by the eukaryotic translation initiation factor 5A eIF5A, a small protein with two isoforms eIF5A-1 and -2, which is highly conserved among eukaryotes, particularly around a unique hypusine residue 1, 2. The putative eukaryotic translation initiation factor 5A eIF5A 1 is an intriguing protein, because it is the only cellular protein known to contain the unique amino acid hypusine, a modification that appears to be required for cell proliferation 1–3.The protein was originally described as a translation initiation factor because of its ability to stimulate the synthesis of methionyl.

The eukaryotic translation initiation factor 5A eIF5A is a protein ubiquitously present in archaea and eukarya, which undergoes a unique two-step post-translational modification called hypusination. The putative eukaryotic translation initiation factor 5A eIF5A is an essential protein for cell viability and the only cellular protein known to contain the unusual amino acid residue hypusine. eIF5A eukaryotic translation initiation factor 5A is the only cellular protein containing hypusine [Nϵ-4-amino-2-hydroxybutyllysine]. eIF5A is activated by the post-translational synthesis of hypusine and the hypusine modification is essential for cell proliferation.

Jul 01, 2007 · Eukaryotic initiation factor 5A eIF5A 1 is a protein found in all eukaryotic cells and archaea,, and is the only known protein that contains the unusual amino acid hypusine N ε -4-amino-2R-hydroxybutyllysine. The synthesis of hypusine within eIF5A is. Eukaryotic translation initiation factor 5A eIF5A is the only cellular protein that contains the unusual amino acid hypusine [N ε- 4-amino-2-hydroxybutyllysine]. The role of hypusine formation. May 01, 2004 · Mature eukaryotic initiation factor 5A eIF5A is the only known protein in eukaryotic cells that contains the unusual amino acid hypusine Nε - 4-amino-2 R-hydroxybutyllysine. The synthesis of hypusine is essential for the function of eIF5A in eukaryotic cell proliferation and survival. The eukaryotic translation initiation factor 5A eIF5A is the only cellular protein containing hypusine, [N ε-4-amino-2-hydroxybutyllysine]. eIF5A is activated by the posttranslational synthesis of hypusine and the hypusine modification is essential for cell proliferation.In this study, we report selective acetylation of the hypusine and/or deoxyhypusine residue of eIF5A by a key polyamine. Eukaryotic translation initiation factor eIF5A has been implicated in HIV-1 replication. This protein contains the apparently unique amino acid hypusine that is formed by the post-translational modification of a lysine residue catalyzed by deoxyhypusine synthase and deoxyhypusine hydroxylase DOHH.

Biochemistry and function of hypusine formation on eukaryotic initiation factor. 5A. Biological Signals. 1997; 6:105–109. Eukaryotic translation initiation factor 5A eIF5A is essential for. The evolutionarily conserved mRNA translation factor eIF5A is critical for cell proliferation in developmental and oncogenic contexts, and its activity depends on hypusination, a posttranslational modification that is unique to eIF5A. Levasseur et al. found that eIF5A hypusination was critical for postnatal expansion of β cell mass in the pancreas. Mice that could not perform hypusination in. Skip to main content. UFDC Home UF Institutional Repository UF Theses & Dissertations Internet Archive UF Institutional Repository UF Theses & Dissertations Internet Archive. Hypusine plays a key role in the regulation of eIF‐5A function because eIF‐5A precursors, which do not contain hypusine, have little, if any, activity []. Moreover, the Lys50→Arg variant is unable to stimulate methionyl‐puromycin synthesis in vitro[[90, 91]] and is inactive in vivo[]. These data suggest that hypusine synthesis is.

Hypusine Formation on Eukaryotic Initiation Factor 5A: Biochemistry and Function (Biological Signals Ser. Series, 3)

Identification of mRNA that binds to eukaryotic initiation.

Hypusine [N epsilon-4-amino-2-hydroxybutyllysine] occurs in all eukaryotes at one residue in a highly conserved protein, the putative eukaryotic translation initiation factor 5A eIF-5A, old. Chen KY, Liu AY. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biological Signals. 1997; 6:105–109. Grigorenko NA, Khomutov AR, Keinänen TA, Järvinen A, Alhonen L, Jänne J, Vepsäläinen J. Synthesis of novel optical isomers of alpha-methylpolyamines. Tetrahedron. 2007; 63:2257–2262. Apr 14, 2004 · 1. Introduction. Hypusine [N ε-4-amino-2hydroxybutyllysine] is an unusual amino acid residue exclusively found in the initiation factor 5A of eukaryotes and archaea eIF-5A and aIF-5A, respectively Park et al., 1981, Bartig et al., 1992, Park et al., 1993, Park et al., 1997.It results of a post-translational modification of a specific lysine residue in this protein Lys 50 in the human. Hypusine modification of the eukaryotic initiation factor 5A eIF-5A is emerging as a crucial regulator in cancer, infections, and inflammation. Although its contribution in translational regulation of proline repeat-rich proteins has been sufficiently demonstrated, its biological role in higher eukaryotes remains poorly understood.

Among a broad range of functions, the polyamine spermidine is needed to hypusinate the translation factor eukaryotic initiation factor 5A eIF5A. We show here that hypusinated eIF5A eIF5A H promotes the efficient expression of a subset of mitochondrial proteins involved in the TCA cycle and oxidative phosphorylation OXPHOS. Jun 21, 2008 · The putative translation initiation factor 5A eIF5A is a small protein, highly conserved and essential in all organisms from archaea to mammals. Although the involvement of eIF5A in translation initiation has been questioned, new evidence reestablished the connection between eIF5A and this cellular process. In order to better understand the function of elF5A, a screen for synthetic lethal. Oct 12, 2013 · Eukaryotic initiation factor 5A eIF5A, the only known cellular protein containing the amino acid hypusine, is an essential component of translation elongation. eIF5A2, one of the two isoforms in the eIF5A family, is reported to be a novel oncogenic protein in many types of human cancer. Chen KY and Liu AY 1997. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol. Signals 6: 105-109. Christianson TW, Sikorski RS, Dante M, Shero JH, et al. 1992. Multifunctional yeast high-copy-number shuttle vectors. Gene 110: 119-122. Clague MJ 1998. Molecular aspects of the endocytic pathway. Biochem. Aug 22, 2010 · The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A eIF5A. J. Biochem. 139, 161–169 2006.

Background: Eukaryotic initiation factor 5A elF-5A contains an unusual amino acid, hypusine [Nϵ-4-aminobutyl-2-hydroxylysine]. The first step in the post-translational formation of hypusine is catalysed by the enzyme deoxyhypusine synthase DHS. The modified version of elF-5A, and DHS, are required for eukaryotic cell proliferation. Knowledge of the three-dimensional structure of this. Eukaryotic translation initiation factor 5A eIF 5A is required for lipidation of ATG 8 proteins and autophagosome formation. This results from eIF 5A‐mediated translation of the E2‐like ATG 3 protein, which contains an amino acid motif causing eIF 5A dependency for its efficient translation. Post-translational modification PTM refers to the covalent and generally enzymatic modification of proteins following protein biosynthesis.Proteins are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo PTM to form the mature protein product. PTMs are important components in cell signaling, as for example when prohormones are converted to hormones. The eukaryotic initiation factor 5A eIF5A, 1 a small 17.4-kDa protein, is activated by a post-translational modification of a specific lysine residue to hypusine N ε-4-amino-2-hydroxybutyllysine in an enzyme-catalyzed two-step mechanism reviewed in Refs. 1 and 2.In the first step, the aminobutyl moiety of the polyamine spermidine is transferred by deoxyhypusine synthase EC 1.1.1.249. Sep 01, 2009 · Deoxyhypusine hydroxylase is the key enzyme in the biosynthesis of hypusine containing eukaryotic translation initiation factor 5A eIF5A, which plays an essential role in the regulation of cell proliferation. Recombinant human deoxyhypusine hydroxylase hDOHH has been reported to have oxygen- and iron-dependent activity, an estimated iron/holoprotein stoichiometry of 2, and a visible.

Dimerization of the yeast eukaryotic translation.

A cDNA encoding a eukaryotic translation initiation factor 5A eIF-5A homolog in heterotrophic dinoflagellate Crypthecodinium cohnii CceIF-5A was isolated through random sequencing of a cDNA library. The predicted amino acid sequence possesses the 12 strictly conserved amino acids around lysine 52 equivalent to lysine 50 or 51 in other eukaryotes. A single 1.2-kb band was detected in.

  1. Only one cellular protein, the eukaryotic initiation factor 5A eIF-5A, is known to contain the modified amino acid residue, termed hypusine. Molecular genetic and pharmacological studies indicate that this modification is essential for cell survival and proliferation.
  2. Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene. It is the only known protein to contain the unusual amino acid hypusine [N ε- 4-amino-2-hydroxybutyl-lysine], which is synthesized on eIF5A at a specific lysine residue from the polyamine spermidine by two catalytic steps. EF-P is the prokaryotic homolog of eIF5A, which is also.

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