The role of mammalian initiation factor eIF-4D and its hypusine modification in translation

John W.B. Hershey, Zeljka McBride, Joachim Schnier

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Initiation factor eIF-4D functions late in the initiation pathway, apparently during formation of the first peptide bond. The factor is post-translationally modified at a specific lysine residue by reaction with spermidine and subsequent hydroxylation to form hypusine. A precursor form lacking hypusine is inactive in the assay for methionyl-puromycin synthesis, but activity is restored following in vitro modification to deoxyhypusine, thereby suggesting that the modification is essential for function. Since formylated methionyl-tRNA is less dependent on eIF-4D in the puromycin assay, we postulate that eIF-4D and its hypusine modification may stabilize charged Met-tRNA binding to the peptidyl transferase center of the 60S ribosomal subunit. Analysis of eIF-4D genes in yeast indicate that eIF-4D and its hypusine modification are essential for cell growth.

Original languageEnglish (US)
Pages (from-to)160-162
Number of pages3
JournalBBA - Gene Structure and Expression
Volume1050
Issue number1-3
DOIs
StatePublished - Aug 27 1990

Fingerprint

Peptide Initiation Factors
Puromycin
Assays
Eukaryotic Large Ribosome Subunits
RNA, Transfer, Met
Peptidyl Transferases
Hydroxylation
Spermidine
Cell growth
Transfer RNA
Yeast
Lysine
Genes
Yeasts
hypusine
eukaryotic translation initiation factor 5A
Peptides
Growth

Keywords

  • Hypusine
  • Initiation factor
  • Protein synthesis
  • Puromycin
  • Yeast

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

Cite this

The role of mammalian initiation factor eIF-4D and its hypusine modification in translation. / Hershey, John W.B.; McBride, Zeljka; Schnier, Joachim.

In: BBA - Gene Structure and Expression, Vol. 1050, No. 1-3, 27.08.1990, p. 160-162.

Research output: Contribution to journalArticle

@article{6463598f7024412ab879d2de04c2b5d5,
title = "The role of mammalian initiation factor eIF-4D and its hypusine modification in translation",
abstract = "Initiation factor eIF-4D functions late in the initiation pathway, apparently during formation of the first peptide bond. The factor is post-translationally modified at a specific lysine residue by reaction with spermidine and subsequent hydroxylation to form hypusine. A precursor form lacking hypusine is inactive in the assay for methionyl-puromycin synthesis, but activity is restored following in vitro modification to deoxyhypusine, thereby suggesting that the modification is essential for function. Since formylated methionyl-tRNA is less dependent on eIF-4D in the puromycin assay, we postulate that eIF-4D and its hypusine modification may stabilize charged Met-tRNA binding to the peptidyl transferase center of the 60S ribosomal subunit. Analysis of eIF-4D genes in yeast indicate that eIF-4D and its hypusine modification are essential for cell growth.",
keywords = "Hypusine, Initiation factor, Protein synthesis, Puromycin, Yeast",
author = "Hershey, {John W.B.} and Zeljka McBride and Joachim Schnier",
year = "1990",
month = "8",
day = "27",
doi = "10.1016/0167-4781(90)90159-Y",
language = "English (US)",
volume = "1050",
pages = "160--162",
journal = "Biochimica et Biophysica Acta - Gene Structure and Expression",
issn = "0167-4781",
publisher = "Elsevier BV",
number = "1-3",

}

TY - JOUR

T1 - The role of mammalian initiation factor eIF-4D and its hypusine modification in translation

AU - Hershey, John W.B.

AU - McBride, Zeljka

AU - Schnier, Joachim

PY - 1990/8/27

Y1 - 1990/8/27

N2 - Initiation factor eIF-4D functions late in the initiation pathway, apparently during formation of the first peptide bond. The factor is post-translationally modified at a specific lysine residue by reaction with spermidine and subsequent hydroxylation to form hypusine. A precursor form lacking hypusine is inactive in the assay for methionyl-puromycin synthesis, but activity is restored following in vitro modification to deoxyhypusine, thereby suggesting that the modification is essential for function. Since formylated methionyl-tRNA is less dependent on eIF-4D in the puromycin assay, we postulate that eIF-4D and its hypusine modification may stabilize charged Met-tRNA binding to the peptidyl transferase center of the 60S ribosomal subunit. Analysis of eIF-4D genes in yeast indicate that eIF-4D and its hypusine modification are essential for cell growth.

AB - Initiation factor eIF-4D functions late in the initiation pathway, apparently during formation of the first peptide bond. The factor is post-translationally modified at a specific lysine residue by reaction with spermidine and subsequent hydroxylation to form hypusine. A precursor form lacking hypusine is inactive in the assay for methionyl-puromycin synthesis, but activity is restored following in vitro modification to deoxyhypusine, thereby suggesting that the modification is essential for function. Since formylated methionyl-tRNA is less dependent on eIF-4D in the puromycin assay, we postulate that eIF-4D and its hypusine modification may stabilize charged Met-tRNA binding to the peptidyl transferase center of the 60S ribosomal subunit. Analysis of eIF-4D genes in yeast indicate that eIF-4D and its hypusine modification are essential for cell growth.

KW - Hypusine

KW - Initiation factor

KW - Protein synthesis

KW - Puromycin

KW - Yeast

UR - http://www.scopus.com/inward/record.url?scp=0025087875&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025087875&partnerID=8YFLogxK

U2 - 10.1016/0167-4781(90)90159-Y

DO - 10.1016/0167-4781(90)90159-Y

M3 - Article

C2 - 2119810

AN - SCOPUS:0025087875

VL - 1050

SP - 160

EP - 162

JO - Biochimica et Biophysica Acta - Gene Structure and Expression

JF - Biochimica et Biophysica Acta - Gene Structure and Expression

SN - 0167-4781

IS - 1-3

ER -