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Cellular coexistence of two high molecular subsets of eEF1B complex
Author(s) -
Le Sourd Frédéric,
Cormier Patrick,
Bach Stéphane,
Boulben Sandrine,
Bellé Robert,
Mulner-Lorillon Odile
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.04.038
Subject(s) - chemistry , microbiology and biotechnology , computational biology , biophysics , biology
The elongation factor eEF1B involved in protein translation was found to contain two isoforms of the eEF1Bδ subunit in sea urchin eggs. The eEF1Bδ2 isoform differs from eEF1Bδ1 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 eEF1Bδ2 antibodies. Quantification of the proteins in immunoprecipitates and on immunoblots demonstrates that eEF1Bδ1 and eEF1Bδ2 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.