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Related Experiment Videos

Three phosphorylation sites in elongation factor 2.

L P Ovchinnikov1, L P Motuz, P G Natapov

  • 1Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.

FEBS Letters
|November 26, 1990
PubMed
Summary

Rabbit reticulocyte elongation factor 2 (EF-2) can be phosphorylated by EF-2 kinase in vitro. This phosphorylation occurs at three specific threonine residues near the N-terminus of EF-2.

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Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Enzymology

Background:

  • Elongation factor 2 (EF-2) is crucial for protein synthesis.
  • EF-2 kinase is involved in regulating protein synthesis through EF-2 phosphorylation.
  • Understanding the specific sites of EF-2 phosphorylation is key to elucidating its regulatory mechanisms.

Purpose of the Study:

  • To identify the specific phosphorylation sites on rabbit reticulocyte EF-2.
  • To characterize the region of EF-2 targeted by EF-2 kinase.
  • To confirm the in vitro phosphorylation capacity of identified threonine residues.

Main Methods:

  • In vitro phosphorylation of EF-2 using partially purified EF-2 kinase and [gamma-32P]ATP.
  • Tryptic hydrolysis of phosphorylated EF-2.

Related Experiment Videos

  • Two-dimensional peptide mapping and high-performance liquid chromatography (HPLC) for phosphopeptide analysis.
  • Peptide sequencing to determine the primary structure of phosphopeptides.

    • Main Results:

    • Four distinct phosphopeptides were generated after tryptic digestion of phosphorylated EF-2.
    • Peptide mapping and sequencing revealed that all phosphopeptides originated from a single N-terminal region of EF-2.
    • This region contains three threonine residues: Thr-53, Thr-56, and Thr-58.
    • Direct phosphate localization confirmed that all three threonine residues can be phosphorylated in vitro.

    Conclusions:

    • Rabbit reticulocyte EF-2 is phosphorylated by EF-2 kinase at Thr-53, Thr-56, and Thr-58 in vitro.
    • These threonine residues are located in a specific N-terminal region of EF-2.
    • The findings provide precise molecular details regarding the regulation of EF-2 activity.