elongation factor


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elongation factor

[ē‚loŋ′gā·shən ‚fak·tər]
(biochemistry)
Any of several proteins required for elongation of growing polypeptide chains during protein synthesis.
References in periodicals archive ?
Eukaryotic Elongation Factor One Alpha (eEF1A) is a multifunctional protein active in protein synthesis and degradation, binding actin and microtubules and several different signal transduction pathways in the cell.
ADP-ribosylation of elongation factor 2 by diphtheria toxin: NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products.
Name of Corresponding Homologous gene after BLAST searching cDNA clone genomic clone (% nucleotide sequence identity) STUB1 9-1 Hordeum vulgare alpha-tubulin 3 (90%) accession number AJ132399 SPRP1 10-1,14-1 Zea mays proline-rich protein (84%) accession number Y17332 SAQ1 16-1 Zea mays plasma membrane MIP protein (pip2) (96%) accession number AF131201 SEF1[alpha] 19-1 Zea mays Elongation factor 1[alpha] (93%) accession number U76259
The trade-offs are not associated with overexpression of the gene for elongation factor.
The researchers' analysis also suggests that the way poxA and yjeK modify the bacterial protein elongation factor is essential in the production of proteins that allow the bacteria to use alternative energy sources when they are deprived of nutrients, as occurs after they enter host cells.
Five enzymes/proteins were identified as being differentially expressed in the livers of ketotic cows: expression of 3-hydroxyacyl-CoA dehydrogenase type-2 (HCDH), acetylcoenzyme A acetyltransferase 2 (ACAT) and elongation factor Tu (EF-Tu) were down-regulated, whereas that of alpha-enolase and creatine kinase were up-regulated.
Our previous studies have shown that enolase, [alpha]- and [beta]-tubulin, and elongation factor 1[beta] are myosin-V binding partners by affinity isolation.
A relationship between the accumulation of elongation factor lA (eEF1A) and endosperm protein-bound lysine in cereals has been established (Habben et al.
Biological and biophysical data using cancer cells resistant or sensitive to Aplidin show that eukaryotic elongation factor 1A2 (eEF1A2) is physically bound to the drug Aplidin.
Selective inhibition of positive transcription elongation factor b (P-TEFb) may add a new key mechanism of action to current cancer therapies via the suppression of anti-apoptotic signals.
We previously identified four different ribosomal protein mRNAs and two different elongation factor mRNAs in rat OL processes (2, 7).