Interaction of wheat protein synthesis elongation factor 1 with GTP analogs
Wheat protein synthesis elongation factor 1 was tested for binding to GTP analogs, including structures resembling "caps" that are present at the 5′-termini of most eukaryotic mRNAs. The interaction was assayed by determining the capacity of the analogs to inhibit the binding of [3H]GTP to elongation factor 1. Significant interaction of elongation factor 1 with G(5′)ppp(5′)G, G(5′)pppp(5′)G, and G(5′)ppp(5′)A was observed. Methylation of a ribose 2′-hydroxyl had very little effect, but methylation of the 7 position of guanosine greatly diminished the affinity of elongation factor 1 for these compounds. m7G(5′)ppp(5′)Cm, m7G(5′)ppp(5′)Um, and m7G(5′)ppp(5′)Am gave no detectable binding with EF1. © 1978.
Artículo de publicación SCOPUS
Quote ItemArchives of Biochemistry and Biophysics, Volumen 187, Issue 2, 2018, Pages 335-338