Immunogold localization of the intracellular sites of structural and nonstructural tobacco mosaic virus proteins

Hills, G. J.; Plaskitt, Kitty A.; Young, Nevin D.; Dunigan, David D.; Watts, J. W.; Wilson, T. M. A.; Zaitlin, Milton

doi:10.1016/0042-6822(87)90143-7

Cited by 91 publications

(56 citation statements)

References 36 publications

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“…For tobamoviruses, the membranes on which the replication complexes reside remain controversial. Immunostaining tobamovirus-infected cells with anti-replication protein antibodies has demonstrated that the replication proteins are localized to cytoplasmic granular inclusion bodies, 69) in ER-associated inclusion, designated X-bodies, 70) and on the ER. 71) However, recent analyses suggest that only a fraction of the ToMV replication proteins are associated with membranes and involved in replication, while the remaining proteins are not associated with membranes, and have no detectable ToMV RNA synthesis activity in vitro.…”

Section: )mentioning

confidence: 99%

Replication of tobamovirus RNA

Ishikawa

Okada

2004

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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Section: )mentioning

confidence: 99%

Replication of tobamovirus RNA

Ishikawa

Okada

2004

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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“…They are composed of aggregates of tubules, embedded in a ribosome-rich matrix Hills et al 1987). The viroplasms contain the 126-kDa and/or 183-kDa replication proteins, which are associated with the tubules and therefore are the likely sites of RNA replication.…”

Section: The Role Of Membranes In the Synthesismentioning

confidence: 99%

Replication of tobacco mosaic virus RNA

Buck

1999

Phil. Trans. R. Soc. Lond. B

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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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“…Tissue blocks of about 2 mm 3 were taken from the tip region and midsection of 2-to 4-d-old etiolated maize coleoptiles and fixed overnight in 2% (w/v) glutaraldehyde in 0.1 M sodium cacodylate, pH 7.2, then lowtemperature embedded as described previously (Wells, 1985;Hills et al, 1987). Thin sections (100 nm) were cut on an ultramicrotome (Leica) and picked up on carbon-coated and plastic-filmed gold grids.…”

Section: Transmission Electron Microscopy and Immunocytochemistrymentioning

confidence: 99%

The Maize Mixed-Linkage (1→3),(1→4)-β-d-Glucan Polysaccharide Is Synthesized at the Golgi Membrane

Carpita

McCann

2010

Plant Physiology

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With the exception of cellulose and callose, the cell wall polysaccharides are synthesized in Golgi membranes, packaged into vesicles, and exported to the plasma membrane where they are integrated into the microfibrillar structure. Consistent with this paradigm, several published reports have shown that the maize (Zea mays) mixed-linkage (1→3),(1→4)-β-d-glucan, a polysaccharide that among angiosperms is unique to the grasses and related Poales species, is synthesized in vitro with isolated maize coleoptile Golgi membranes and the nucleotide-sugar substrate, UDP-glucose. However, a recent study reported the inability to detect the β-glucan immunocytochemically at the Golgi, resulting in a hypothesis that the mixed-linkage β-glucan oligomers may be initiated at the Golgi but are polymerized at the plasma membrane surface. Here, we demonstrate that (1→3),(1→4)-β-d-glucans are detected immunocytochemically at the Golgi of the developing maize coleoptiles. Further, when maize seedlings at the third-leaf stage were pulse labeled with [14C]O2 and Golgi membranes were isolated from elongating cells at the base of the developing leaves, (1→3),(1→4)-β-d-glucans of an average molecular mass of 250 kD and higher were detected in isolated Golgi membranes. When the pulse was followed by a chase period, the labeled polysaccharides of the Golgi membrane diminished with subsequent transfer to the cell wall. (1→3),(1→4)-β-d-Glucans of at least 250 kD were isolated from cell walls, but much larger aggregates were also detected, indicating a potential for intermolecular interactions with glucuronoarabinoxylans or intermolecular grafting in muro.

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Immunogold localization of the intracellular sites of structural and nonstructural tobacco mosaic virus proteins

Cited by 91 publications

References 36 publications

Replication of tobamovirus RNA

Replication of tobamovirus RNA

Replication of tobacco mosaic virus RNA

The Maize Mixed-Linkage (1→3),(1→4)-β-d-Glucan Polysaccharide Is Synthesized at the Golgi Membrane

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