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Changes in eIF-4D hypusine modification or abundance are not correlated with translational repression in HeLa cells.

Abstract
Initiation factor eIF-4D is represented by about 11 X 10(6) molecules/HeLa cell (0.45% of the cytoplasmic protein molecules). The fraction of eIF-4D that contains the post-translational modification of lysine converted to hypusine is not regulated with respect to translation rate in HeLa cells. It is proportional to the rate of eIF-4D synthesis in exponentially growing cells (maximal protein synthesis rates) as well as in serum-depleted cells (protein synthesis rates depressed about 6-8-fold). In cells in which protein synthesis is arrested by cycloheximide, no hypusine addition or exchange is detected. During rapid repressions of protein synthesis due to either heat shock or hypertonic shock there is no change in the extent of eIF-4D containing hypusine. These results are most consistent with an eIF-4D biogenesis in which all molecules are modified to contain hypusine during or shortly after the translation process itself, and the modification state is not regulated thereafter.
AuthorsR F Duncan, J W Hershey
JournalThe Journal of biological chemistry (J Biol Chem) Vol. 261 Issue 27 Pg. 12903-6 (Sep 25 1986) ISSN: 0021-9258 [Print] UNITED STATES
PMID3091607 (Publication Type: Journal Article)
Chemical References
  • Peptide Initiation Factors
  • RNA-Binding Proteins
  • Saline Solution, Hypertonic
  • eukaryotic translation initiation factor 5A
  • hypusine
  • Lysine
Topics
  • Electrophoresis, Polyacrylamide Gel
  • HeLa Cells (metabolism)
  • Hot Temperature
  • Humans
  • Lysine (analogs & derivatives, metabolism)
  • Peptide Initiation Factors (metabolism)
  • Protein Biosynthesis
  • RNA-Binding Proteins
  • Saline Solution, Hypertonic

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