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
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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).
Item Type: |
Journal Article (Original Article) |
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Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine |
Graduate School: |
Graduate School for Cellular and Biomedical Sciences (GCB) |
UniBE Contributor: |
Arndt, Nick Willy, Ross, Daniela, Altmann, Michael |
Subjects: |
500 Science > 570 Life sciences; biology 600 Technology > 610 Medicine & health |
ISSN: |
2045-2322 |
Publisher: |
Nature Publishing Group |
Language: |
English |
Submitter: |
Dr. Nick Willy Arndt |
Date Deposited: |
04 Jun 2018 14:07 |
Last Modified: |
05 Dec 2022 15:14 |
Publisher DOI: |
10.1038/s41598-018-25273-3 |
PubMed ID: |
29712996 |
BORIS DOI: |
10.7892/boris.116932 |
URI: |
https://boris.unibe.ch/id/eprint/116932 |
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