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

Abstract 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 p...

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Autores principales:	Nick Arndt, Daniela Ross-Kaschitza, Artyom Kojukhov, Anton A. Komar, Michael Altmann
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3a6728c6bc13469d9e09f51aeaea2ff4
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spelling	oai:doaj.org-article:3a6728c6bc13469d9e09f51aeaea2ff42021-12-02T12:32:36ZProperties of the ternary complex formed by yeast eIF4E, p20 and mRNA10.1038/s41598-018-25273-32045-2322https://doaj.org/article/3a6728c6bc13469d9e09f51aeaea2ff42018-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-25273-3https://doaj.org/toc/2045-2322Abstract 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).Nick ArndtDaniela Ross-KaschitzaArtyom KojukhovAnton A. KomarMichael AltmannNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nick Arndt Daniela Ross-Kaschitza Artyom Kojukhov Anton A. Komar Michael Altmann Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA
description	Abstract 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).
format	article
author	Nick Arndt Daniela Ross-Kaschitza Artyom Kojukhov Anton A. Komar Michael Altmann
author_facet	Nick Arndt Daniela Ross-Kaschitza Artyom Kojukhov Anton A. Komar Michael Altmann
author_sort	Nick Arndt
title	Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA
title_short	Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA
title_full	Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA
title_fullStr	Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA
title_full_unstemmed	Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA
title_sort	properties of the ternary complex formed by yeast eif4e, p20 and mrna
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/3a6728c6bc13469d9e09f51aeaea2ff4
work_keys_str_mv	AT nickarndt propertiesoftheternarycomplexformedbyyeasteif4ep20andmrna AT danielarosskaschitza propertiesoftheternarycomplexformedbyyeasteif4ep20andmrna AT artyomkojukhov propertiesoftheternarycomplexformedbyyeasteif4ep20andmrna AT antonakomar propertiesoftheternarycomplexformedbyyeasteif4ep20andmrna AT michaelaltmann propertiesoftheternarycomplexformedbyyeasteif4ep20andmrna
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Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA

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