The Role of the Poly(A) binding protein in the assembly of the Cap-binding complex during translation initiation in plants

Gallie, Daniel

doi:10.4161/trla.29630

Cited by 7 publications

(13 citation statements)

References 117 publications

(156 reference statements)

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“…Extensive biochemical and kinetic characterization of the interactions of wheat eIF4B, eIF4A, eIF4G/eIFiso4G and PABP confirm that the interactions are similar to other organisms (reviewed in Gallie, 2014;Le et al, 1997;Khan and Goss, 2005;Gallie, 2006, 2007;Cheng et al, 2008;Khan et al, 2008;Khan et al, 2009;Mayberry et al, 2009;Cheng and Gallie, 2010;Yumak et al, 2010;Khan and Goss, 2012;Cheng and Gallie, 2013). Wheat eIF4B has two tandem domains for interaction with eIF4A and PABP separated by a RNA binding domain in addition to binding domains for eIF4G/iso4G and eIF3g.…”

Section: Eif4bmentioning

confidence: 99%

“…This suggests that eIF4B may interact with more than one molecule of eIF4A or PABP at a time during initiation events. Further, the interactions with eIF4G/iso4G and eIF4A appear to be specific to plant eIF4B, suggesting divergent evolution of this factor from other eukaryotes (Gallie, 2014). eIF4B also assists eIF3 in CaMV infection and the TAV-mediated reinitiation on the 35S transcript.…”

Section: Eif4bmentioning

confidence: 99%

“…Plant eIFiso4G and eIF4G domains have been mapped and shown to have similar types of interactions with eIF4A, eIF4B and PAPB, but have some differences from the mammalian or yeast interactions (Gallie, 2014). Further structural details will be required to understand how similar or different these plant factor interactions are to other eukaryotes.…”

Section: Eif4g and Eifiso4gmentioning

confidence: 99%

“…Several recent reviews on translation provide mechanistic and structural details of translation derived with S. cerevisiae and mammalian systems (Sonenberg and Hinnebusch, 2009;Jackson et al, 2010;Lorsch and Dever, 2010;Hinnebusch, 2011;Aitken and Lorsch, 2012;Dever and Green, 2012;Hernán-dez et al, 2012;Hershey et al, 2012;Hinnebusch and Lorsch, 2012;Valasek, 2012;Voigts-Hoffmann et al, 2012;Lomakin and Steitz, 2013;Hinnebusch, 2014;Mead et al, 2014;Merrick and Harris, 2014). Translation in plants has been reviewed with different emphases in the past five years Muench et al, 2012;Muñoz and Castellano, 2012;Echevarría-Zomeño et al, 2013;Browning, 2014;Gallie, 2014), and several historical reviews provide the back story (Browning, 1996;Bailey-Serres, 1999;Kawaguchi and Bailey-Serres, 2002;Browning, 2004;Gallie, 2007). As will be described, the translational machinery of plants resembles that of S. cerevisiae and mammals.…”

Section: Act 1: Initiation Of Translationmentioning

confidence: 99%

“…Extensive biochemical analysis of wheat PABP has shown that the presence of eIF4G or eIF4B enhances its RNA binding activity and in turn the presence of PABP increases the affinity of the eIF4F complex for the cap and stimulates the ATPase and RNA helicase activities of eIF4A, eIF4F/eIFiso4F and eIF4B (reviewed in Gallie, 2014;Le et al, 1997;Wei et al, 1998;Luo and Goss, 2001;Khan and Goss, 2005;Cheng and Gallie, 2010). It has been further shown that plant eIF4G has an additional PABP binding domain that binds eIF4B in a competitive and mutually exclusive manner (Cheng and Gallie, 2010;Cheng and Gallie, 2013).…”

Section: Poly(a) Binding Proteinmentioning

confidence: 99%

See 4 more Smart Citations

Mechanism of Cytoplasmic mRNA Translation

Browning

Bailey‐Serres

2015

The Arabidopsis Book

187

220

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Protein synthesis is a fundamental process in gene expression that depends upon the abundance and accessibility of the mRNA transcript as well as the activity of many protein and RNA-protein complexes. Here we focus on the intricate mechanics of mRNA translation in the cytoplasm of higher plants. This chapter includes an inventory of the plant translational apparatus and a detailed review of the translational processes of initiation, elongation, and termination. The majority of mechanistic studies of cytoplasmic translation have been carried out in yeast and mammalian systems. The factors and mechanisms of translation are for the most part conserved across eukaryotes; however, some distinctions are known to exist in plants. A comprehensive understanding of the complex translational apparatus and its regulation in plants is warranted, as the modulation of protein production is critical to development, environmental plasticity and biomass yield in diverse ecosystems and agricultural settings.

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Section: Eif4bmentioning

confidence: 99%

Section: Eif4bmentioning

confidence: 99%

Section: Eif4g and Eifiso4gmentioning

confidence: 99%

Section: Act 1: Initiation Of Translationmentioning

confidence: 99%

Section: Poly(a) Binding Proteinmentioning

confidence: 99%

See 3 more Smart Citations

Mechanism of Cytoplasmic mRNA Translation

Browning

Bailey‐Serres

2015

The Arabidopsis Book

187

220

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Phosphorylation and interactions associated with the control of theLeishmaniaPoly-A Binding Protein 1 (PABP1) function during translation initiation

et al. 2018

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2018)Phosphorylation and interactions associated with the control of the Leishmania Poly-A Binding Protein 1 (PABP1) function during translation initiation, RNA Biology, 15:6, 739-755, ABSTRACTThe Poly-A Binding Protein (PABP) is a conserved eukaryotic polypeptide involved in many aspects of mRNA metabolism. During translation initiation, PABP interacts with the translation initiation complex eIF4F and enhances the translation of polyadenylated mRNAs. Schematically, most PABPs can be divided into an N-terminal RNA-binding region, a non-conserved linker segment and the C-terminal MLLE domain. In pathogenic Leishmania protozoans, three PABP homologues have been identified, with the first one (PABP1) targeted by phosphorylation and shown to co-immunoprecipitate with an eIF4F-like complex (EIF4E4/EIF4G3) implicated in translation initiation. Here, PABP1 phosphorylation was shown to be linked to logarithmic cell growth, reminiscent of EIF4E4 phosphorylation, and coincides with polysomal association. Phosphorylation targets multiple serine-proline (SP) or threonine-proline (TP) residues within the PABP1 linker region. This is an essential protein, but phosphorylation is not needed for its association with polysomes or cell viability. Mutations which do impair PABP1 polysomal association and are required for viability do not prevent phosphorylation, although further mutations lead to a presumed inactive protein largely lacking phosphorylated isoforms. Co-immunoprecipitation experiments were carried out to investigate PABP1 function further, identifying several novel protein partners and the EIF4E4/EIF4G3 complex, but no other eIF4F-like complex or subunit. A novel, direct interaction between PABP1 and EIF4E4 was also investigated and found to be mediated by the PABP1 MLLE binding to PABP Interacting Motifs (PAM2) within the EIF4E4 N-terminus. The results shown here are consistent with phosphorylation of PABP1 being part of a novel pathway controlling its function and possibly translation in Leishmania.

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Molecular crosstalk between plant translation initiation complexes influences the outcome of virus infection

Zafirov

Giovinazzo

Lecampion

et al. 2023

Preprint

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Successful subversion of translation initiation factors 4E and 4G determines the infection success of potyviruses, the largest group of viruses affecting plants. In the natural variability of many plant species, resistance to potyvirus infection is provided by polymorphisms at 4E and 4G that renders them inadequate for virus hijacking but still functional in translation initiation. In crops where such natural resistance alleles are limited, the genetic inactivation of 4E has been proposed for the engineering of potyvirus resistance. However, recent findings indicate that knockout 4E and 4G alleles may be deleterious for plant health and could jeopardize resistance efficiency in comparison to functional resistance proteins. Here, we explored the cause of these adverse effects by studying the role of the Arabidopsis eIF4E1, whose inactivation was previously reported as conferring resistance to the potyvirus clover yellow vein virus (ClYVV) while also promoting susceptibility to another potyvirus called turnip mosaic virus (TuMV). We report that eIF4E1 is required to maintain global plant translation and to restrict TuMV accumulation during infection, and its absence is associated with a favoured virus multiplication over host translation. Furthermore, our findings demonstrate that eIF4E1 plays a crucial role in inhibiting the TuMV-induced degradation of the translation initiation factor eIFiso4G1, thereby preventing the generation of a truncated protein. Finally, we demonstrate a role for eIFiso4G1 in TuMV accumulation and in supporting plant fitness during infection. These findings suggest that eIF4E1 counteracts the hijacking of the plant translational apparatus during TuMV infection and underscore the importance of preserving the functionality of translation initiation factors 4E and 4G when implementing potyvirus resistance strategies.

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The Role of the Poly(A) binding protein in the assembly of the Cap-binding complex during translation initiation in plants

Cited by 7 publications

References 117 publications

Mechanism of Cytoplasmic mRNA Translation

Mechanism of Cytoplasmic mRNA Translation

Phosphorylation and interactions associated with the control of theLeishmaniaPoly-A Binding Protein 1 (PABP1) function during translation initiation

Molecular crosstalk between plant translation initiation complexes influences the outcome of virus infection

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