Nucleic acid-binding properties of the alfalfa mosaic virus movement protein produced in yeast

Schoumacher, Fabrice; Erny, Claude; Berna, Anne; Godefroy-Colburn, T.; Stussi-Garaud, C.

doi:10.1016/0042-6822(92)90549-5

Cited by 66 publications

(30 citation statements)

References 16 publications

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“…HC-Pro RNA-binding activity is stable at ionic strengths up to 400 mM-NaCI and is inactivated by heat. The behaviour of RNA binding to HC-Pro is reminiscent of RNA-protein interactions believed to reflect co-operative processes (Citovsky et al, 1990;Osman et al, 1992;Schoumacher et al, 1992;Soumounou & Lalibert6, 1994). However, in view of recent results obtained by Thomas & Maule (1995) with the gene I protein of cauliflower mosaic virus (CaMV), identification of a co-operative RNA-binding activity using mobility-shift assays should be interpreted with caution.…”

Section: Discussionmentioning

confidence: 99%

“…No detectable complex (lane 2) was formed with MBP:fl-gal~ and possible minor contaminant E. coli protein(s). Furthermore, no apparent alteration in the electrophoretic mobility of the cross-linked complex versus the non- cross-linked fusion protein was observed, as is the case for other virus RNA-binding proteins (Citovsky et al, 1990;Schoumacher et al, 1992). Second, Northwestern blot assays were performed to determine whether RNA-binding activity could be associated with genuine HC-Pro (Fig.…”

Section: Determination Of the Rna-binding Properties Of Mbp :Hc-promentioning

confidence: 99%

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Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase

Maia

Bernardi

1996

Journal of General Virology

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The potyvirus helper component-proteinase (HC-Pro) is a multifunctional protein previously reported to have affinity for polyribonucleotides. To investigate further the ability of HC-Pro to bind nucleic acids, the potato virus Y (PVY) LYE84 isolate HC-Pro gene was amplified, cloned in an Escherichia coli expression vector and sequenced. HC-Pro was expressed as a fusion with the maltose-binding protein and purified by affinity chromatography. Electrophoretic mobility-shift assays demonstrated that HC-Pro acts as a sequence nonspecific RNA-binding protein and suggest that more than one molecule of protein was bound per molecule of RNA. The HC-Pro RNA-binding activity was stable in 400 mu-NaC1 and temperature sensitive. The recombinant protein preferentially bound ssRNA over DNA or dsRNA and showed little, if any, affinity for poly(A). The possible implications of the RNA-binding activity of HC-Pro in potyvirus replication and movement are discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Determination Of the Rna-binding Properties Of Mbp :Hc-promentioning

confidence: 99%

Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase

Maia

Bernardi

1996

Journal of General Virology

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“…This TMVlike mechanism for cell-to-cell movement may complement the previously characterized spread of CaMV in the form of whole viral particles through virus-modi¢ed plasmodesmata (Kitajima & Lauritis 1969). In addition to TMV and CaMV, the movement proteins of alfalfa mosaic virus (AMV), red clover necrotic mosaic dianthovirus (RCNMV) and several other viruses have been shown to bind single-stranded nucleic acids (Osman et al 1992;Schoumacher et al 1992;Pascal et al 1994). As with TMV P30, these movement proteins bound nucleic acids cooperatively (Citovsky et al 1991;Osman et al 1992;Schoumacher et al 1992); however, the movement protein of RCNMV did not appear to lengthen bound RNA molecules signi¢cantly (Fujiwara et al 1993).…”

Section: Movement Protein±nucleic Acid Complexesmentioning

confidence: 93%

“…In addition to TMV and CaMV, the movement proteins of alfalfa mosaic virus (AMV), red clover necrotic mosaic dianthovirus (RCNMV) and several other viruses have been shown to bind single-stranded nucleic acids (Osman et al 1992;Schoumacher et al 1992;Pascal et al 1994). As with TMV P30, these movement proteins bound nucleic acids cooperatively (Citovsky et al 1991;Osman et al 1992;Schoumacher et al 1992); however, the movement protein of RCNMV did not appear to lengthen bound RNA molecules signi¢cantly (Fujiwara et al 1993). Thus, transport through plasmodesmata via movement proteinn ucleic acid intermediates may represent a common mechanism for cell-to-cell spread of many plant viruses.…”

Section: Movement Protein±nucleic Acid Complexesmentioning

confidence: 99%

Tobacco mosaic virus: a pioneer to cell–to–cell movement

Citovsky

1999

Phil. Trans. R. Soc. Lond. B

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Cell-to-cell movement of tobacco mosaic virus (TMV) is used to illustrate macromolecular tra¤c through plant intercellular connections, the plasmodesmata. This transport process is mediated by a specialized viral movement protein, P30. In the initially infected cell, P30 is produced by transcription of a subgenomic RNA derived from the invading virus. Presumably, P30 then associates with a certain proportion of the viral RNA molecules, sequestering them from replication and mediating their transport into neighbouring uninfected host cells. This nucleoprotein complex is targeted to plasmodesmata, possibly via interaction with the host cell's cytoskeleton. Prior to passage through a plasmodesma, the plasmodesmatal channel is dilated by the movement protein. It is proposed that targeting of P30-TMV RNA complexes to plasmodesmatal involves binding to a speci¢c cell-wall-associated receptor molecule. This protein, designated p38, also functions as a protein kinase, phosphorylating P30 at its carboxyterminus and minimizing P30-induced interference with plasmodesmatal permeability during viral infection.

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“…However, observations made in vitro and in vivo have allowed the assignment of several activities and characteristics to the protein. The MP, when expressed in and purified from E. coli, binds single-stranded nucleic acid cooperatively but with no sequence specificity (Citovsky et al, 1990(Citovsky et al, , 1992, as do MPs of several other viruses (Citovsky et al, 1991;Ivanov et al, 1994;Osman et al, 1992;Rouleau et al, 1994;Schoumacher et al, 1992). The MP binds GTP specifically in vitro (Li and Palukaitis, 1996).…”

Section: Introductionmentioning

confidence: 99%

Domains of the TMV movement protein involved in subcellular localization

et al. 1998

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SummaryTo identify and map functionally important regions of the tobacco mosaic virus movement protein, deletions of three amino acids were introduced at intervals of 10 amino acids throughout the protein. Mutations located between amino acids 1 and 160 abolished the capacity of the protein to transport virus from cell to cell, while some of the mutations in the C-terminal third of the protein permitted function. Despite extensive tests, no examples were found of intermolecular complementation between mutants, suggesting that function requires each movement protein molecule to be fully competent. Many of the mutants were fused to green fluorescent protein, and their subcellular localizations were determined by fluorescence microscopy in infected plants and protoplasts. Most mutants lost the ability to accumulate in one or more of the multiple subcellular sites targeted by wild-type movement protein, suggesting that specific functional domains were disrupted. The order in which accumulation at subcellular sites occurs during infection does not represent a targeting pathway. Association of the movement protein with microtubules or with plasmodesmata can occur in the absence of other associations. The region of the protein around amino acids 9-11 may be involved in targeting the protein to cortical bodies (probably associated with the endoplasmic reticulum) and to plasmodesmata. The region around residues 49-51 may be involved in co-alignment of the protein with microtubules. The region around residues 88-101 appears to play a role in targeting to both the cortical bodies and microtubules. Thus, the movement protein contains independently functional domains.

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Nucleic acid-binding properties of the alfalfa mosaic virus movement protein produced in yeast

Cited by 66 publications

References 16 publications

Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase

Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase

Tobacco mosaic virus: a pioneer to cell–to–cell movement

Domains of the TMV movement protein involved in subcellular localization

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