Coordinated and selective recruitment of eIF4E and eIF4G factors for potyvirus infection in <i>Arabidopsis thaliana</i>

Nicaise, Valérie; Gallois, Jean‐Luc; Chafiai, Faccila; Allen, Leah M.; Schurdi‐Levraud, Valérie; Browning, Karen S.; Candresse, Thierry; Caranta, Carole; Gall, Olivier Le; German-Retana, Sylvie

doi:10.1016/j.febslet.2007.02.007

Cited by 113 publications

(117 citation statements)

References 30 publications

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“…S4). However, a redundant role of these two isoforms in regulating the translation of HSA32 could not be excluded, as we did not check the triple KO mutant of eIF4G, eIF (iso)4G1, and eIF(iso)4G2, which could be lethal in Arabidopsis (Nicaise et al, 2007). In addition to translation, HSP101 may retard the degradation of HSA32.…”

Section: Discussionmentioning

confidence: 99%

“…The double KO mutant hsp101 hsa32-1 was generated by crossing the single mutant lines and isolated from the offspring in the F2 generation. The T-DNA KO mutant of eIF4G and double KO mutants of eIF(iso)4G1 and eIF(iso)4G2 were described in detail previously (Nicaise et al, 2007) and confirmed by PCR analysis with gene-specific primers. EMS-mutagenized M2 seeds (Columbia [Col-0] ecotype) were purchased from Lehle Seeds.…”

Section: Plants Materials and Mutant Screenmentioning

confidence: 99%

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Interplay between Heat Shock Proteins HSP101 and HSA32 Prolongs Heat Acclimation Memory Posttranscriptionally in Arabidopsis

Juan

Hsu

et al. 2013

Plant Physiology

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Heat acclimation improves the tolerance of organisms to severe heat stress. Our previous work showed that in Arabidopsis (Arabidopsis thaliana), the "memory" of heat acclimation treatment decayed faster in the absence of the heat-stress-associated 32-kD protein HSA32, a heat-induced protein predominantly found in plants. The HSA32 null mutant attains normal short-term acquired thermotolerance but is defective in long-term acquired thermotolerance. To further explore this phenomenon, we isolated Arabidopsis defective in long-term acquired thermotolerance (dlt) mutants using a forward genetic screen. Two recessive missense alleles, dlt1-1 and dlt1-2, encode the molecular chaperone heat shock protein101 (HSP101). Results of immunoblot analyses suggest that HSP101 enhances the translation of HSA32 during recovery after heat treatment, and in turn, HSA32 retards the decay of HSP101. The dlt1-1 mutation has little effect on HSP101 chaperone activity and thermotolerance function but compromises the regulation of HSA32. In contrast, dlt1-2 impairs the chaperone activity and thermotolerance function of HSP101 but not the regulation of HSA32. These results suggest that HSP101 has a dual function, which could be decoupled by the mutations. Pulse-chase analysis showed that HSP101 degraded faster in the absence of HSA32. The autophagic proteolysis inhibitor E-64d, but not the proteasome inhibitor MG132, inhibited the degradation of HSP101. Ectopic expression of HSA32 confirmed its effect on the decay of HSP101 at the posttranscriptional level and showed that HSA32 was not sufficient to confer long-term acquired thermotolerance when the HSP101 level was low. Taken together, we propose that a positive feedback loop between HSP101 and HSA32 at the protein level is a novel mechanism for prolonging the memory of heat acclimation.

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Section: Discussionmentioning

confidence: 99%

Section: Plants Materials and Mutant Screenmentioning

confidence: 99%

Interplay between Heat Shock Proteins HSP101 and HSA32 Prolongs Heat Acclimation Memory Posttranscriptionally in Arabidopsis

Juan

Hsu

et al. 2013

Plant Physiology

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“…In A. thaliana, four genes [eIF4E1, eIF4E2, eIF4E3 and eIF(iso)4E] encode proteins of the eIF4E family and three genes [eIF4G, eIF4(iso)G1 and eIF4(iso)G2] encode proteins of the eIF4G family (http://research.cm.utexas.edu/kbrowning/fiat/). The different isoforms appear to carry out complementary biological functions as demonstrated by the lack of specific phenotypes in plants with disrupted eIF4E/4G isomers (Duprat et al, 2002;Nicaise et al, 2007;Sato et al, 2005). An analogous role for PABP is demonstrated here, as individual deletion of constitutive and highly expressing PABP paralogues (i.e.…”

Section: Discussionmentioning

confidence: 75%

“…As seen with TuMV and other potyviruses, the disruption of eukaryotic translation initiation factors such as eIF4E/ eIFiso4E and eIF4G/eIF(iso)4G in A. thaliana leads to potyvirus resistance (Duprat et al, 2002;Lellis et al, 2002;Nicaise et al, 2007) which is indicative of their absolute requirement for virus infection.…”

Section: Isolation Of Viable Single and Double Pab T-dna Insertion Mumentioning

confidence: 99%

“…Similar results were also obtained using IRES derived from the Tobacco etch virus (Gallie, 2001;Gallie et al, 1995 , 1997) and disruption of the interaction leads to resistance (Léonard et al, 2000). Requirement for eIF4E/4G or eIF(iso)4E/4G isomers depends on the virus being studied, as A. thaliana knockout plants for eIF(iso)4E or eIF(iso)4G1/2 genes are resistant to TuMV, lettuce mosaic virus and plum pox virus infection, while disruption of eIF4E1 or eIF4G results in resistance to clover yellow vein virus (Decroocq et al, 2006; Duprat et al, 2002;Lellis et al, 2002;Nicaise et al, 2007;Sato et al, 2005). These results were also confirmed in multiple plant species with the identification of eIF4E and eIF4G isoforms as recessive resistance gene products against potyviruses (Gao et al, 2004;Kang et al, 2005;Nicaise et al, 2003; Ruffel et al, 2002Ruffel et al, , 2005.…”

Section: Introductionmentioning

confidence: 99%

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Arabidopsis thaliana class II poly(A)-binding proteins are required for efficient multiplication of turnip mosaic virus

Dufresne

Ubalijoro

Fortin

et al. 2008

Journal of General Virology

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The poly(A)-binding protein (PABP) is an important translation initiation factor that binds to the polyadenylated 39 end of mRNA. We have previously shown that PABP2 interacts with the RNAdependent RNA polymerase (RdRp) and VPg-Pro of turnip mosaic virus (TuMV) within virusinduced vesicles. At least eight PABP isoforms are produced in Arabidopsis thaliana, three of which (PABP2, PABP4 and PABP8) are highly and broadly expressed and probably constitute the bulk of PABP required for cellular functions. Upon TuMV infection, an increase in protein and mRNA expression from PAB2, PAB4 and PAB8 genes was recorded. In vitro binding assays revealed that RdRp and the viral genome-linked protein (VPg-Pro) interact preferentially with PABP2 but are also capable of interaction with one or both of the other class II PABPs (i.e. PABP4 and PABP8). To assess whether PABP is required for potyvirus replication, A. thaliana single and double pab knockouts were isolated and inoculated with TuMV. All lines showed susceptibility to TuMV. However, when precise monitoring of viral RNA accumulation was performed, it was found to be reduced by 2.2-and 3.5-fold in pab2 pab4 and pab2 pab8 mutants, respectively, when compared with wild-type plants. PABP levels were most significantly reduced in the membrane-associated fraction in both of these mutants. TuMV mRNA levels thus correlated with cellular PABP concentrations in these A. thaliana knockout lines. These data provide further support for a role of PABP in potyvirus replication. INTRODUCTIONThe poly(A)-binding protein (PABP) is an abundant translation initiation factor in the cell that binds to the polyadenylated 39 end of mRNA. Its interaction with the eukaryotic translation initiation factor 4F complex (composed of the eIF4E, eIF4A and eIF4G proteins), which is bound to the 59 cap structure of the mRNA, results in the formation of a protein bridge that brings the 59 and 39 termini of the mRNA into proximity. This leads to a synergistic enhancement of translation (Sachs, 2000;Wells et al., 1998). PABP is also important for stability (BehmAnsmant et al., 2007;Parker & Song, 2004), biogenesis (Amrani et al., 1997;Brown & Sachs, 1998) and nuclear export of cellular mRNAs (Brune et al., 2005).Multiple PABP isoforms are normally found in animals and plants (Mangus et al., 2003). Eight PABP genes have been identified in Arabidopsis thaliana (Belostotsky, 2003).The corresponding proteins are divided into four classes based on gene expression and similarity. Class II genes (PAB2, PAB4 and PAB8) are highly and broadly expressed and probably encode the bulk of PABP required for cellular functions (Belostotsky, 2003).In animal cells, PABP is cleaved by proteinases of picornaviruses (Joachims et al., 1999;Kerekatte et al., 1999;Kuyumcu-Martinez et al., 2002, 2004bRodriguez Pulido et al., 2007;Zhang et al., 2007), caliciviruses (Kuyumcu-Martinez et al., 2004a) and retroviruses (Alvarez et al., 2006). The resultant cleavage leads to host translational shutdown (Joachims et al., 1999; KuyumcuMartinez ...

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Plant Resistance to Infection by Viruses

Nicaise¹,

Revers²

2007

Encyclopedia of Life Sciences

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Damages caused by viruses have a major economic and agronomic impact in agriculture. To counter these attacks, plants have developed efficient defence mechanisms that prevent or limit viral infection. Recently, important advances in our understanding of the molecular nature and mechanisms associated with recessive or dominant natural virus resistance genes have been made, as well as concerning the general antiviral defence system based on ribonucleic acid (RNA) silencing.

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Coordinated and selective recruitment of eIF4E and eIF4G factors for potyvirus infection in Arabidopsis thaliana

Cited by 113 publications

References 30 publications

Interplay between Heat Shock Proteins HSP101 and HSA32 Prolongs Heat Acclimation Memory Posttranscriptionally in Arabidopsis

Interplay between Heat Shock Proteins HSP101 and HSA32 Prolongs Heat Acclimation Memory Posttranscriptionally in Arabidopsis

Arabidopsis thaliana class II poly(A)-binding proteins are required for efficient multiplication of turnip mosaic virus

Plant Resistance to Infection by Viruses

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