Ca2+/calmodulin-dependent phosphorylation of elongation factor 2

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

Incubation of a ribosome-free extract of rabbit reticulocytes or rat liver with [γ-32P]ATP and Ca2+ results in incorporation of 32P predominantly into a single polypeptide of Mr ∼ 100 000. This polypeptide is identified as elongation factor 2 (EF-2). Phosphorylation of EF-2 is strictly Ca2+-dependent and can be inhibited by the calmodulin antagonist trifluoperazine. It is suggested that the Ca2+/calmodulin-dependent phosphorylation of EF-2 is involved in regulation of protein biosynthesis.

Original languageEnglish (US)
Pages (from-to)331-334
Number of pages4
JournalFEBS Letters
Volume214
Issue number2
DOIs
StatePublished - Apr 20 1987
Externally publishedYes

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Peptide Elongation Factor 2
Phosphorylation
Calmodulin
Trifluoperazine
Peptides
Reticulocytes
Biosynthesis
Protein Biosynthesis
Ribosomes
Liver
Rats
Adenosine Triphosphate
Rabbits
Proteins

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

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abstract = "Incubation of a ribosome-free extract of rabbit reticulocytes or rat liver with [γ-32P]ATP and Ca2+ results in incorporation of 32P predominantly into a single polypeptide of Mr ∼ 100 000. This polypeptide is identified as elongation factor 2 (EF-2). Phosphorylation of EF-2 is strictly Ca2+-dependent and can be inhibited by the calmodulin antagonist trifluoperazine. It is suggested that the Ca2+/calmodulin-dependent phosphorylation of EF-2 is involved in regulation of protein biosynthesis.",
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Ca2+/calmodulin-dependent phosphorylation of elongation factor 2. / Ryazanov, Alexey.

In: FEBS Letters, Vol. 214, No. 2, 20.04.1987, p. 331-334.

Research output: Contribution to journalArticle

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PY - 1987/4/20

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AB - Incubation of a ribosome-free extract of rabbit reticulocytes or rat liver with [γ-32P]ATP and Ca2+ results in incorporation of 32P predominantly into a single polypeptide of Mr ∼ 100 000. This polypeptide is identified as elongation factor 2 (EF-2). Phosphorylation of EF-2 is strictly Ca2+-dependent and can be inhibited by the calmodulin antagonist trifluoperazine. It is suggested that the Ca2+/calmodulin-dependent phosphorylation of EF-2 is involved in regulation of protein biosynthesis.

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