The extreme N-terminal domain of a hordeivirus TGB1 movement protein mediates its localization to the nucleolus and interaction with fibrillarin

Semashko, Maria; González, Inmaculada; Shaw, Jane; Леонова, О.Г.; Попенко, В. И.; Taliansky, Michael; Canto, Tomás; Калинина, Н. В.

doi:10.1016/j.biochi.2012.02.005

Cited by 34 publications

(31 citation statements)

References 39 publications

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“…With the exception of Rubisco, which remained enriched in band 1, the most abundant host protein precipitating with anti-P20 IgG was a nucleolar protein, fibrillarin, which was detected in band 2 in three independent experiments (Table 1). Fibrillarin is known to interact with viral MPs and is important for long-distance trafficking of several RNA viruses (Kim et al, 2007;Taliansky et al, 2010;Semashko et al, 2012;Zheng et al, 2015). The LC-MS/MS results were confirmed by immunoblot analysis, revealing the presence of P20 and fibrillarin in the P20 co-IP complex in the HV coinfected tissues (Figures 4C and 4D).…”

Section: Host Factors Immunoprecipitated With P20 Proteinmentioning

confidence: 60%

“…Thus, viruses must have evolved various strategies to interact with cellular factors to be loaded into and unloaded from the vascular system (Chen et al, 2000;Kim et al, 2007;Harries et al, 2009;Raffaele et al, 2009;Taliansky et al, 2010;Semashko et al, 2012;Hipper et al, 2013). Host factors such as myosin are required for MP targeting to and virus movement through the PD (Amari et al, 2014;Harries et al, 2009); intercellular and long-distance trafficking of Tobacco mosaic virus (TMV) (Chen et al, 2000) and Groundnut rosette virus (GRV) (Kim et al, 2007;Taliansky et al, 2010;Semashko et al, 2012) were substantially delayed in plants silenced for PECTIN METHYLESTERASE and fibrillarin. However, remorin, a Solanaceae protein resident in membrane rafts and plasmodesmata, can interact physically with the MP from Potato virus X and negatively regulates Potato virus X intercellular and phloem-mediated trafficking (Raffaele et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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The Nucleolar Fibrillarin Protein Is Required for Helper Virus-Independent Long-Distance Trafficking of a Subviral Satellite RNA in Plants

et al. 2016

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RNA trafficking plays pivotal roles in regulating plant development, gene silencing, and adaptation to environmental stress. Satellite RNAs (satRNAs), parasites of viruses, depend on their helper viruses (HVs) for replication, encapsidation, and efficient spread. However, it remains largely unknown how satRNAs interact with viruses and the cellular machinery to undergo trafficking. Here, we show that the P20 protein of Bamboo mosaic potexvirus satRNA (satBaMV) can functionally complement in trans the systemic trafficking of P20-defective satBaMV in infected Nicotiana benthamiana. The transgenederived satBaMV, uncoupled from HV replication, was able to move autonomously across a graft union identified by RT-qPCR, RNA gel blot, and in situ RT-PCR analyses. Coimmunoprecipitation experiments revealed that the major nucleolar protein fibrillarin is coprecipitated in the P20 protein complex. Notably, silencing fibrillarin suppressed satBaMV-, but not HV-, phloem-based movement following grafting or coinoculation with HV. Confocal microscopy revealed that the P20 protein colocalized with fibrillarin in the nucleoli and formed punctate structures associated with plasmodesmata. The mobile satBaMV RNA appears to exist as ribonucleoprotein (RNP) complex composed of P20 and fibrillarin, whereas BaMV movement proteins, capsid protein, and BaMV RNA are recruited with HV coinfection. Taken together, our findings provide insight into movement of satBaMV via the fibrillarin-satBaMV-P20 RNP complex in phloem-mediated systemic trafficking.

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Section: Host Factors Immunoprecipitated With P20 Proteinmentioning

confidence: 60%

Section: Introductionmentioning

confidence: 99%

The Nucleolar Fibrillarin Protein Is Required for Helper Virus-Independent Long-Distance Trafficking of a Subviral Satellite RNA in Plants

et al. 2016

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“…Although this observation could be an artifact of overexpression, one plausible explanation for this is that there is a direct interaction between V2 and Fib2. Several plant RNA viruses and human RNA and DNA viruses have been shown to interact with fibrillarin or other nucleolar components (i.e., nucleolin) [6][7][8][9][10][11][12][13]. The association of V2 with the nucleolus and CBs is intriguing and needs further investigation.…”

Section: Resultsmentioning

confidence: 97%

Subcellular localization of grapevine red blotch-associated virus ORFs V2 and V3

et al. 2015

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Grapevine red blotch-associated virus is a recently discovered plant monopartite gemini-like virus found in North American grapevines. Leaf discoloration and a decrease in fruit quality are associated with its infection. Two of its six open reading frames (ORFs), V2 and V3, are of unknown function and share no obvious homology with plant or viral genes. Transient expression of these ORFs in fusion with the green fluorescent protein demonstrated that the V2 protein localizes in the nucleoplasm, Cajal bodies, and cytoplasm; and the V3 protein localizes in various unidentified subnuclear bodies. Additionally, the V2 protein is redirected to the nucleolus upon co-expression with the nucleolus and Cajal body-associated protein Fib2.

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“…Our results show that only a single nucleolar localization motif is present in OuMV CP. Only a few cases of plant viral proteins targeted to the nucleolus have been reported, and the NoLSs that have been characterized so far are rich in positively charged amino acids [2,7,8,11,19,20,[23][24][25][26]. Alfalfa mosaic virus (AMV), for instance, has a short NoLS that is rich in lysine and arginine residues at the N-terminus of the CP, which, in addition to its role as a sorting signal, acts as modulator of RNA binding and it is responsible for cell-to-cell and longdistance movement of AMV [8].…”

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confidence: 99%

Genetic dissection of a putative nucleolar localization signal in the coat protein of ourmia melon virus

2013

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Ourmiaviruses became the object of recent attention for their unusual taxonomic placements among plant viruses. The ourmia melon virus (OuMV) RNA3 encodes a 22-kDa coat protein (CP). Besides its role in virion formation, the OuMV CP facilitates systemic virus spread. In Nicotiana benthamiana, an eGFP-CP fusion protein was localized in the nucleus and preferentially in the nucleolus. By bioinformatics analysis, we identified an arginine-and lysine-rich region at the N-terminus of the CP. Here, we demonstrate by deletion and alanine scanning mutagenesis that this region in the CP is responsible for its preferential accumulation in the nucleolus of host cells.

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The extreme N-terminal domain of a hordeivirus TGB1 movement protein mediates its localization to the nucleolus and interaction with fibrillarin

Cited by 34 publications

References 39 publications

The Nucleolar Fibrillarin Protein Is Required for Helper Virus-Independent Long-Distance Trafficking of a Subviral Satellite RNA in Plants

The Nucleolar Fibrillarin Protein Is Required for Helper Virus-Independent Long-Distance Trafficking of a Subviral Satellite RNA in Plants

Subcellular localization of grapevine red blotch-associated virus ORFs V2 and V3

Genetic dissection of a putative nucleolar localization signal in the coat protein of ourmia melon virus

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