The alpha subunit of elongation factor-1 (EEF1A) is involved in the binding of aminoacyl-tRNAs to 80S ribosomes. During the process, GTP is hydrolyzed into GDP. To perform this function, EEF1A has domains that bind guanine nucleotides, 80S ribosomes, and aminoacyl-tRNAs. Also, EEF1A interacts with the beta subunit of EEF1 to exchange bound GDP for GTP. Multimolecular complexes involving the eukaryotic elongation factor 1A (eEF1A) have been suggested to play an important role in the channeling (vectorial transfer) of tRNA during protein synthesis HIV-1 matrix protein (MA) was found to interact with elongation factor 1-α (EF1α), an essential component of the translation machinery that delivers aminoacyl-tRNA to ribosomes. The interaction between MA and EF1α impairs translation in vitro, a result consistent with a previously proposed model in which inhibition of translation by the accumulation of Gag serves to release viral RNA from polysomes, permitting the RNA to be packaged into nascent virions. It has been identified that the translation elongation factor, eEF1A, and its guanine nucleotide exchange factor, eEF1Bβ, as translationally controlled tumor protein (TCTP)-interacting partners.
Forme physique
Clear and colorless frozen liquid solution
Notes préparatoires
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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European journal of biochemistry, 155(1), 167-171 (1986-02-17)
The primary structure of the alpha subunit of elongation factor 1 (EF-1 alpha) from human MOLT 4 cells was determined by cDNA sequencing. The data show that the conservation of the amino acid sequence is more than 80% when compared
Journal of virology, 73(7), 5388-5401 (1999-06-11)
Human immunodeficiency virus type 1 (HIV-1) gag-encoded proteins play key functions at almost all stages of the viral life cycle. Since these functions may require association with cellular factors, the HIV-1 matrix protein (MA) was used as bait in a
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