Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA
| Autor: | N. Arndt, Michael Altmann, Daniela Ross-Kaschitza, Anton A. Komar, Artyom Kojukhov |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Science RNA Stability Eukaryotic Initiation Factor-4E 610 Medicine & health Saccharomyces cerevisiae Ternary Complex Factors Arginine Article 03 medical and health sciences chemistry.chemical_compound otorhinolaryngologic diseases Histidine Amino Acid Sequence RNA Messenger Nucleotide Motifs Binding site Ternary complex Nuclear Cap-Binding Protein Complex Messenger RNA Binding Sites Multidisciplinary EIF4G Nuclear cap-binding protein complex EIF4E Translation (biology) 030104 developmental biology chemistry Biophysics Medicine 570 Life sciences biology Protein Binding |
| Zdroj: | Arndt, Nick; Ross-Kaschitza, Daniela; Kojukhov, Artyom; Komar, Anton A.; Altmann, Michael (2018). Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA. Scientific Reports, 8(1), p. 6707. Nature Publishing Group 10.1038/s41598-018-25273-3 Scientific Reports Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018) |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/s41598-018-25273-3 |
| Popis: | Yeast p20 is a small, acidic protein that binds eIF4E, the cap-binding protein. It has been proposed to affect mRNA translation and degradation, however p20′s function as an eIF4E-binding protein (4E-BP) and its physiological significance has not been clearly established. In this paper we present data demonstrating that p20 is capable of binding directly to mRNA due to electrostatic interaction of a stretch of arginine and histidine residues in the protein with negatively charged phosphates in the mRNA backbone. This interaction contributes to formation of a ternary eIF4E/p20/capped mRNA complex that is more stable than complexes composed of capped mRNA bound to eIF4E in the absence of p20. eIF4E/p20 complex was found to have a more pronounced stimulatory effect on capped mRNA translation than purified eIF4E alone. Addition of peptides containing the eIF4E-binding domains present in p20 (motif YTIDELF), in eIF4G (motif YGPTFLL) or Eap1 (motif YSMNELY) completely inhibited eIF4E-dependent capped mRNA translation (in vitro), but had a greatly reduced inhibitory effect when eIF4E/p20 complex was present. We propose that the eIF4E/p20/mRNA complex serves as a stable depository of mRNAs existing in a dynamic equilibrium with other complexes such as eIF4E/eIF4G (required for translation) and eIF4E/Eap1 (required for mRNA degradation). |
| Databáze: | OpenAIRE |
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