The RNA of Tobacco etch virus: Further characterization and detection of protein linked to RNA

Hari, V.

doi:10.1016/0042-6822(81)90286-5

Cited by 97 publications

(44 citation statements)

References 19 publications

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“…The presence of VPg proteins analogous to those of picornaviruses (see Salas & Vifiuela, 1980) has been demonstrated for CPMV (Daubert et al, 1978;Stanley et al, 1978) and other comoviruses (Daubert & Bruening, 1979), sobemoviruses (Ghosh et al, 1979;Hull & Morris-Krsinich, 1980), potyviruses (Hari, 1981), and nepoviruses (Harrison & Barker, 1978;Mayo et al, 1979). Here again, there is no correlation with the grouping according to monopartite or multicomponent types.…”

Section: ' Terminal Sequencesmentioning

confidence: 85%

Genome Expression of Plant Positive-strand RNA Viruses

Davies

Hull

1982

Journal of General Virology

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Section: ' Terminal Sequencesmentioning

confidence: 85%

Genome Expression of Plant Positive-strand RNA Viruses

Davies

Hull

1982

Journal of General Virology

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“…The potyviral genome has a poly(A) sequence at the 3' end (Hari et al, 1979) and is covalently bound at the 5' end to a protein termed VPg (Hari, 1981;Siaw et al, 1985;Riechmann et al, 1989;Murphy et al, 1990). The tobacco etch potyvirus (TEV) genome nucleotide sequence has been determined (Allison et al, 1986) and contains a single open reading frame that is translated into a large polyprotein, as shown in Figure 1 (Allison et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Nuclear Transport of Plant Potyviral Proteins

Restrepo¹,

Freed²,

Carrington³

1990

The Plant Cell

139

180

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We have used immunoblotting, immunocytochemical, and gene fusion methods to examine the differential subcellular partitioning of tobacco etch potyvirus proteins that are potentially associated with RNA replication. From the earliest timepoints at which viral proteins could be detected, proteins Nla (49-kilodalton proteinase) and Nlb (58-kilodalton polymerase) were localized primarily in the nucleus, whereas the 71-kilodalton cylindrical inclusion protein was identified in the cytoplasm. The Nla and Nlb coding regions were fused to the 8-glucuronidase (GUS) sequence in a plant expression vector, resulting in synthesis of chimeric proteins in transfected protoplasts and in transgenic plants. In situ localization of GUS activity revealed nuclear localization of the GUS-Nla and GUS-NIb fusion proteins and cytoplasmic localization of nonfused GUS. These results indicate that both Nla and Nlb contain nuclear targeting signals, and that they may serve as useful models for studies of plant cell nuclear transport. A discussion of the general utility of the nuclear transport system described here, as well as the role of nuclear translocation of potyviral proteins, is presented.

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“…TEV has been reported to have a 6K VPg associated with its RNA (Hari, 1981), and the 6K protein was originally considered to be the VPg protein of TEV and PVY (Allison et al, 1986;Robaglia et al, 1989). However, the RNAs of TVMV and PPV are thought to be linked to VPgs of 24K (Siaw et al, 1985) and 22K (Riechmann et al, 1989), respectively.…”

Section: Comparison Of Prsv Proteins With Other Potyvirus Proteinsmentioning

confidence: 99%

Complete Nucleotide Sequence and Genetic Organization of Papaya Ringspot Virus RNA

Yeh

Jan

Chiang

et al. 1992

Journal of General Virology

138

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The complete nucleotide sequence of the RNA genome of papaya ringspot virus (PRSV) was determined from four overlapping cDNA clones and by direct sequencing of viral RNA. The genomic RNA is 10326 nucleotides in length, excluding the poly(A) tract, and contains one large open reading frame that starts at nucleotide positions 86 to 88 and ends at positions 10118 to 10120, encoding a polyprotein of 3344 amino acids. The highly conserved sequence AAAUAAAANANCUCAACACAACAUA at the 5' end of the RNA of PRSV and those of the other five reported potyviruses shows 80% similarity, suggesting that this region may play a common important role for potyvirus replication. Two cleavage sites of the polyprotein were determined by amino acid sequencing of the N termini of helper component (HC-Pro, amorphous inclusion) and cylindrical inclusion (CI) proteins. Other cleavage sites were predicted by analogy with the other potyviruses. The genetic organization of PRSV is similar to that of the other potyviruses except that the first protein processed from the N terminus of the polyprotein (NT protein) has an Mr of 63K, 18K to 34K larger than those of the other potyviruses. The cleavage site for liberating the N terminus of the HCPro protein was found at the same location downstream from the consensus sequence FI(V)VRG as that reported for tobacco vein mottling virus. The NT protein of potyviruses is the most variable and may be considered important for identification of individual potyviruses. The most conserved protein ofpotyviruses appears to be the Nlb protein, the putative polymerase for the replication of the potyviral RNA. The genetic organization of PRSV RNA is tentatively proposed to be VPg-5' leader-63K NT-52K HC-Pro-46K-72K CI-6K-48K NIa-59K NIb-35K coat protein-3' noncoding region-poly(A) tract.

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The RNA of Tobacco etch virus: Further characterization and detection of protein linked to RNA

Cited by 97 publications

References 19 publications

Genome Expression of Plant Positive-strand RNA Viruses

Genome Expression of Plant Positive-strand RNA Viruses

Nuclear Transport of Plant Potyviral Proteins

Complete Nucleotide Sequence and Genetic Organization of Papaya Ringspot Virus RNA

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