Identification of Aspartyl-tRNA Synthetase as Co-purifying with Wheat Germ eIF2
Ophelia Papoulas1, Edward M Marcotte1, Karen S Browning1
1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712 USA.
Researchers identified a ~61kDa protein co-purifying with eukaryotic translation initiation factor 2 (eIF2) from wheat germ. This protein was identified as aspartyl-tRNA synthetase, potentially linking translation initiation to cellular stress responses.
Area of Science:
- Molecular Biology
- Protein Biochemistry
Background:
- Eukaryotic translation initiation factor 2 (eIF2) is crucial for protein synthesis.
- Early wheat germ eIF2 preparations consistently contained an unidentified ~61kDa protein.
Purpose of the Study:
- To identify the persistently co-purifying ~61kDa protein associated with eIF2.
- To investigate the functional implications of this protein complex.
Main Methods:
- Mass spectrometry was employed to analyze an archived gel of purified eIF2 from 1991.
- Protein identification was performed using established proteomic techniques.
Main Results:
- The unidentified ~61kDa protein was identified as aspartyl-tRNA synthetase.
- Aspartyl-tRNA synthetase is known to bind the R enantiomer of β-aminobutyric acid.
Conclusions:
- The study identifies aspartyl-tRNA synthetase as a stable component of eIF2 preparations.
- This finding suggests potential stable "super complexes" linking translation initiation with stress responses, possibly via eIF2α phosphorylation pathways.
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