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Cellular coexistence of two high molecular subsets of eEF1B complex
- Source :
- FEBS Letters. (11):2755-2760
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
-
Abstract
- The elongation factor eEF1B involved in protein translation was found to contain two isoforms of the eEF1Bdelta subunit in sea urchin eggs. The eEF1Bdelta2 isoform differs from eEF1Bdelta1 by a specific insert of 26 amino acids. Both isoforms are co-expressed in the cell and likely originate from a unique gene. The feature appears universal in metazoans as judged from in silico analysis in EST-databanks. The eEF1B components were co-immunoprecipitated by specific eEF1Bdelta2 antibodies. Quantification of the proteins in immunoprecipitates and on immunoblots demonstrates that eEF1Bdelta1 and eEF1Bdelta2 proteins are present in two subsets of eEF1B complex. We discuss and propose a model for the different subsets of eEF1B complex concomitantly present in the cell.
- Subjects :
- Gene isoform
Time Factors
Protein subunit
In silico
Cell
Biophysics
Plasma protein binding
Biology
Biochemistry
Isozyme
Peptide Elongation Factor 1
eEF1B
Structural Biology
Genetics
medicine
Animals
Molecular Biology
chemistry.chemical_classification
Protein translation
Sea urchin egg
Gene Expression Regulation, Developmental
Cell Biology
Molecular biology
Amino acid
Cell biology
Elongation factor
Isoenzymes
Molecular Weight
Protein Subunits
medicine.anatomical_structure
chemistry
Multiprotein Complexes
Sea Urchins
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 11
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....c30ba3d07a09c1bc708d528cb50a2934
- Full Text :
- https://doi.org/10.1016/j.febslet.2006.04.038