Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA

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)

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 and 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:

10 Jun 2018 02:29

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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