Distinct domains of Me31B interact with different eIF4E isoforms in the male germ line of <i>Drosophila melanogaster</i>

Eukaryotic translation initiation factor 4E (eIF4E) is a key factor involved in different aspects of mRNA metabolism. <i>Drosophila melanogaster</i> genome encodes eight eIF4E isoforms, and the canonical isoform eIF4E-1 is a ubiquitous protein that plays a key role in mRNA translation. e...

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Autores principales: Layana, Carla, Vilardo, Emiliano Salvador, Corujo, Gonzalo, Hernández, Greco, Rivera Pomar, Rolando Víctor
Formato: Articulo Preprint
Lenguaje:Inglés
Publicado: 2021
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/124539
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id I19-R120-10915-124539
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Bioquímica
Me31B
eIF4E
mRNP
Translation initiation
P-bodies
Drosophila
spellingShingle Ciencias Exactas
Bioquímica
Me31B
eIF4E
mRNP
Translation initiation
P-bodies
Drosophila
Layana, Carla
Vilardo, Emiliano Salvador
Corujo, Gonzalo
Hernández, Greco
Rivera Pomar, Rolando Víctor
Distinct domains of Me31B interact with different eIF4E isoforms in the male germ line of <i>Drosophila melanogaster</i>
topic_facet Ciencias Exactas
Bioquímica
Me31B
eIF4E
mRNP
Translation initiation
P-bodies
Drosophila
description Eukaryotic translation initiation factor 4E (eIF4E) is a key factor involved in different aspects of mRNA metabolism. <i>Drosophila melanogaster</i> genome encodes eight eIF4E isoforms, and the canonical isoform eIF4E-1 is a ubiquitous protein that plays a key role in mRNA translation. eIF4E-3 is specifically expressed in testis and controls translation during spermatogenesis. In eukaryotic cells, translational control and mRNA decay is highly regulated in different cytoplasmic ribonucleoprotein foci, which include the processing bodies (PBs). In this study, we show that <i>Drosophila</i> eIF4E-1 and eIF4E-3 occur in PBs where might play a role in mRNA storage and translational repression. We also demonstrate that the DEAD-box RNA helicase Me31B, a component of PBs, physically interacts with eIF4E-1 and eIF4E-3 both in the yeast two-hybrid system and FRET in <i>Drosophila</i> S2 cells. Moreover, truncated and point mutated Me31B proteins indicate that the binding sites of Me31B for eIF4E-1 and eIF4E-3 are located in different domains. Residues Y401-L407 (at the carboxy-terminal) are essential for interaction with eIF4E-1, whereas residues F63-L70 (at the amino-terminal) are critical for interaction with eIF4E-3. Thus, Me31B represents a novel type of eIF4E-interacting protein. Our observations suggest that Me31B might recognize different eIF4E isoforms in different tissues, which could be the key to silencing specific messengers. They provide further evidence that alternative forms of eIF4E and their interactions with various partners add complexity to the control of gene expression in eukaryotes.
format Articulo
Preprint
author Layana, Carla
Vilardo, Emiliano Salvador
Corujo, Gonzalo
Hernández, Greco
Rivera Pomar, Rolando Víctor
author_facet Layana, Carla
Vilardo, Emiliano Salvador
Corujo, Gonzalo
Hernández, Greco
Rivera Pomar, Rolando Víctor
author_sort Layana, Carla
title Distinct domains of Me31B interact with different eIF4E isoforms in the male germ line of <i>Drosophila melanogaster</i>
title_short Distinct domains of Me31B interact with different eIF4E isoforms in the male germ line of <i>Drosophila melanogaster</i>
title_full Distinct domains of Me31B interact with different eIF4E isoforms in the male germ line of <i>Drosophila melanogaster</i>
title_fullStr Distinct domains of Me31B interact with different eIF4E isoforms in the male germ line of <i>Drosophila melanogaster</i>
title_full_unstemmed Distinct domains of Me31B interact with different eIF4E isoforms in the male germ line of <i>Drosophila melanogaster</i>
title_sort distinct domains of me31b interact with different eif4e isoforms in the male germ line of <i>drosophila melanogaster</i>
publishDate 2021
url http://sedici.unlp.edu.ar/handle/10915/124539
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