Cooperative binding of the red clover necrotic mosaic virus movement protein to single-stranded nucleic acids

Osman, T. A. M.; Hayes, Robert J.; Buck, K. W.

doi:10.1099/0022-1317-73-2-223

Cited by 93 publications

(84 citation statements)

References 24 publications

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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: 94%

“…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%

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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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Section: Movement Protein±nucleic Acid Complexesmentioning

confidence: 94%

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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“…Our investigations demonstrated that CP not only interacted with its natural substrate (RNA), but also with ssDNA. DNA-binding by RNA-binding proteins has been previously reported for the TMV and RCNMV MPs which naturally bind to RNA (Citovsky et al, 1990;Osman et al, 1992).…”

mentioning

confidence: 90%

“…l a). The strength of interaction between RNA and CP was comparable to reported values for the cauliflower mosaic virus (CaMV) gene I product (stable up to 0.15-0-2 M; Citovsky el al., 1991) and the MP of alfalfa mosaic virus (A1MV) (stable up to 0.2 M; Schoumacher et al, 1992), while being weaker than the values reported for the TMV and red clover necrotic mosaic virus (RCNMV) MPs (both stable up to 0.6 M; Citovsky et al, 1990;Osman et al, 1992). Interactions between CPs and RNA had been reported to be stable in salt concentrations up to 0.8 M and 0"5 M for brome mosaic virus (BMV) (Duggal & Hall, 1993) and for turnip crinkle virus (TCV) (Wei & Morris, 1991), respectively.…”

mentioning

confidence: 95%

Cooperative binding to nucleic acids by barley yellow mosaic bymovirus coat protein and characterization of a nucleic acid-binding domain

Reichel

Maas²,

Schulze³

et al. 1996

Journal of General Virology

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The capacity of several coat protein (CP) mutants of a German isolate of barley yellow mosaic bymovirus (BaYMV) to bind to nucleic acids was studied in vitro. Recombinant CP, produced by overexpression in Escherichia eoli, was purified from inclusion bodies and subsequently renatured. Binding to single-stranded (ss) RNA and ssDNA oligonucleotides was found to be cooperative and sequence non-specific. By deletion mutagenesis, several truncated CP derivatives were created and their nucleic acid-binding capacity was investigated in order to define a protein domain responsible for RNA-and DNA-binding. The nucleic acid-binding domain consists of a core which was located to an internal 23 amino acid peptide (aa 125-147) and an adjacent domain (aa 148-184) which stimulates binding.

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“…This work suggests that the dianthovirus RNA-2 encodes the cell-to-cell movement function and more specifically that the RNA-2-encoded 35K polypeptide (Lommel et al, 1988; is the cell-tocell movement protein. This conclusion is supported by the identification of the movement protein in infected plant cell walls and the cooperative ssRNA-binding properties of the protein Osman et al, 1992). Here we report the complete nucleotide sequence of CRSV RNA-2 and compare the deduced amino acid sequence of the putative movement protein with those of two strains of RCNMV.…”

mentioning

confidence: 72%

Nucleotide sequence of carnation ringspot dianthovirus RNA-2

Kendall¹,

Lommel²

1992

Journal of General Virology

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RNA-2 of carnation ringspot virus (CRSV), the type member of the dianthovirus group, has been cDNA cloned and sequenced. CRSV RNA-2 is 1394 nucleotides in length and contains a single open reading frame encoding a 304 amino acid polypeptide of 33-8K. Amino acid sequence alignment of this polypeptide with the cell-to-cell movement proteins encoded by RNA-2 of red clover necrotic mosaic virus (RCNMV) Australian (Aus) and Czechoslovakian (TpM-34) isolates indicates 59.6% and 55-7% sequence identity, respectively. The N-terminal 230 amino acids are more highly conserved, with 64.3% and 62.6% sequence identity, respectively. The cell-to-cell movement proteins of the two RCNMV isolates are themselves 82-5 % and 91-7 % identical when the amino-terminal 230 amino acids are compared. Structural prediction comparison of the RCNMV-Aus, RCNMV-TpM-34 and tobacco mosaic virus cell-to-cell movement proteins to the putative CRSV RNA-2-encoded movement protein suggests that even though no primary amino acid sequence similarity exists, the movement protein polypeptides are possibly similar in structure and function.

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Cooperative binding of the red clover necrotic mosaic virus movement protein to single-stranded nucleic acids

Cited by 93 publications

References 24 publications

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

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

Cooperative binding to nucleic acids by barley yellow mosaic bymovirus coat protein and characterization of a nucleic acid-binding domain

Nucleotide sequence of carnation ringspot dianthovirus RNA-2

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