Sequence of 1000 nucleotides at the 3′ end of tobacco mosaic virus RNA

Guilley, H.; Jonard, G.; Kukla, B.; Richards, K.

doi:10.1093/nar/6.4.1287

Cited by 128 publications

(71 citation statements)

References 41 publications

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“…It is noteworthy that the coat protein subgenomic RNA, like the genomic RNA, is capped (Keith & Fraenkel-Conrat 1975;Zimmern 1975;Guilley et al 1979), whereas indirect evidence (analogue inhibitor studies) suggests that the movement protein subgenomic RNA may not be capped (Hunter et al 1983;Joshi et al 1983).…”

Section: Virus-encoded Proteins Needed For Tmv Rna Replicationmentioning

confidence: 99%

Replication of tobacco mosaic virus RNA

Buck

1999

Phil. Trans. R. Soc. Lond. B

101

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The replication of tobacco mosaic virus (TMV) RNA involves synthesis of a negative-strand RNA using the genomic positive-strand RNA as a template, followed by the synthesis of positive-strand RNA on the negative-strand RNA templates. Intermediates of replication isolated from infected cells include completely double-stranded RNA (replicative form) and partly double-stranded and partly single-stranded RNA (replicative intermediate), but it is not known whether these structures are double-stranded or largely single-stranded in vivo. The synthesis of negative strands ceases before that of positive strands, and positive and negative strands may be synthesized by two di¡erent polymerases. The genomic-length negative strand also serves as a template for the synthesis of subgenomic mRNAs for the virus movement and coat proteins. Both the virus-encoded 126-kDa protein, which has amino-acid sequence motifs typical of methyltransferases and helicases, and the 183-kDa protein, which has additional motifs characteristic of RNA-dependent RNA polymerases, are required for e¤cient TMV RNA replication. Puri¢ed TMV RNA polymerase also contains a host protein serologically related to the RNA-binding subunit of the yeast translational initiation factor, eIF3. Study of Arabidopsis mutants defective in RNA replication indicates that at least two host proteins are needed for TMV RNA replication. The tomato resistance gene Tm-1 may also encode a mutant form of a host protein component of the TMV replicase. TMV replicase complexes are located on the endoplasmic reticulum in close association with the cytoskeleton in cytoplasmic bodies called viroplasms, which mature to produce`X bodies'. Viroplasms are sites of both RNA replication and protein synthesis, and may provide compartments in which the various stages of the virus mutiplication cycle (protein synthesis, RNA replication, virus movement, encapsidation) are localized and coordinated. Membranes may also be important for the con¢guration of the replicase with respect to initiation of RNA synthesis, and synthesis and release of progeny single-stranded RNA.

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Section: Virus-encoded Proteins Needed For Tmv Rna Replicationmentioning

confidence: 99%

Replication of tobacco mosaic virus RNA

Buck

1999

Phil. Trans. R. Soc. Lond. B

101

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“…Although essentially correct (Hunter et al, 1976;Guilley et al, 1979), their experimental conclusions relied heavily upon two mutually dependent, false assumptions.…”

Section: Discussionmentioning

confidence: 99%

“…This long-standing anomaly can now be resolved. Specifically encapsidated RNA fragments from the coat gene (positions 294 to 398 from the 3'-end of TMV RNA; Guilley et al, 1979) could be exposed in a subpopulation of bidirectionally uncoated rods, after limited stripping for less than 500 nucleotides from the 3'-terminus.…”

Section: Discussionmentioning

confidence: 99%

“…Similar results have been reported for overlapping 3'-terminal subgenomic fragments of TMV RNA prepared by stripping in alkali and the 30K gene was tentatively located by this method. Detailed sequence information (Guilley et al, 1979; G. P. Lomonossoff, unpublished results) has revealed the location of this gene between nucleotides 686 to 1500 (approx.) from the 3'-end.…”

Section: Cell-free Protein Synthesismentioning

confidence: 95%

“…Spots 1, 4 and 5 are clearly present in all four RNA fractions (there is perhaps some decrease in the amount of spot 1 in fraction D). Oligonucleotide positions are known for the 3'-terminal sequence of TMV (Guilley et al, 1979): 1 lies between bases 976 and 992, 4 between bases 563 and 579, and 5 between bases 510 and 525 (from the 3'-hydroxyl terminus). The persistence of these oligonucleotides in all fractions demonstrates that any stripping from the 3'-end of the RNA cannot have proceeded for more than 500 bases.…”

Section: Sequence Analysis Of Rna Contained In Tmv Rods Partially Strmentioning

confidence: 99%

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Dimethyl Sulphoxide (DMSO) Disassembles Tobacco Mosaic Virus Predominantly from the 5'-end of the Viral RNA

Wilson

Lomonossoff

Glover

1981

Journal of General Virology

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SUMMARYThe effect of dimethyl sulphoxide (DMSO) on the stability of native and EDTA-treated tobacco mosaic virus (TMV, Vulgare strain) has been reinvestigated using a variety of chemical and biochemical techniques. Contrary to earlier reports, we conclude that TMV rods behave as a heterodisperse population, exhibiting one of two modes of uncoating. More than 50% of the rods disassemble rapidly and extensively in a unique polar fashion beginning at the 5'-end of the viral RNA. The remainder of the rod population uncoats more slowly, less extensively, and exhibits substantial bidirectional exposure of the viral RNA, commencing at the 3'-terminus but proceeding for no more than 500 nucleotides before the major uncoating event again shifts to the 5'-ends of the particles. A portion of the coat protein gene and the region around the assembly initiation site on the viral RNA appears most resistant to uni-or bidirectional stripping; this is in contrast to previous reports. This complex, biphasic behaviour of the TMV rod population, which produces two broad and relatively ill-defined peaks of metastable nucleoprotein intermediates, may account for many of the inconsistencies prevalent in earlier work.

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The tRNA-like structure of turnip yellow mosaic virus RNA: structural organization of the last 159 nucleotides from the 3′ OH terminus

et al. 1982

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The secondary structure of the isolated tRNA‐like sequence (n=159) present at the 3′ OH terminus of turnip yellow mosaic virus RNA has been established from partial nuclease digestion with S1 nuclease and T1, CL3, and Naja oxiana RNases. The fragment folds into a 6‐armed structure with two main domains. The first domain, of loose structure and nearest the 5′ OH terminus, is composed of one large arm which extends into the coat protein cistron. The second, more compact domain, is composed of the five other arms and most probably contains the structure recognized by valyl‐tRNA synthetase. In this domain three successive arms strikingly resemble the T[unk], anticodon, and D arms found in tRNA. Near the amino‐acid accepting terminus, however, there is a new stem and loop region not found in standard tRNA. This secondary structure is compatible with a L‐shaped three‐dimensional organization in which the corner of the L and the anticodon‐containing limb are similar to, and the amino‐acid accepting region different from, that in tRNA. Ethylnitrosourea accessibility studies have shown similar tertiary structure features in the T[unk] loop of tRNAVal and in the homologous region of the viral RNA.

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Sequence of 1000 nucleotides at the 3′ end of tobacco mosaic virus RNA

Cited by 128 publications

References 41 publications

Replication of tobacco mosaic virus RNA

Replication of tobacco mosaic virus RNA

Dimethyl Sulphoxide (DMSO) Disassembles Tobacco Mosaic Virus Predominantly from the 5'-end of the Viral RNA

The tRNA-like structure of turnip yellow mosaic virus RNA: structural organization of the last 159 nucleotides from the 3′ OH terminus

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