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At least 253 records · Page 14Linked to original sources
PubMed1998

Domains of the TMV movement protein involved in subcellular localization.

To 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.

Amino Acid Sequence↗
PubMed1988

Characterization of the TMV encapsidation initiation site on 18S rRNA.

Tobacco Mosaic Virus capsid protein oligomers react with and encapsidate 18S rRNA from both plant and mammalian sources in vitro. The site (ei) in 18S rRNA which reacts with capsid protein to initiate the packaging reaction has been localized and partially characterized by testing the ability of transcripts from different regions of a cloned Cucurbita pepo rDNA repeat unit to become encapsidated. The 18S rRNA ei is found to react more slowly with capsid protein than does the functional virion ei and to lie within a 43 nucleotide region which starts at position 157 from the 5' terminus of 18S rRNA. When 6 nucleotides are removed from the 5' end, the remaining 37 nucleotide segment is still reactive, but with reduced efficiency. The primary structure of the reactive segment has limited similarity to the virion ei and can be folded into a stem-loop. The first 18 nucleotides of the ei region is highly conserved from an evolutionary standpoint and this may account for the ability of 18S rRNAs from both plant and mammalian sources to be encapsidated.

Capsid↗
PubMed1996

Expression of class I O-methyltransferase in healthy and TMV-infected tobacco.

Tobacco possesses two distinct classes of O-methyltransferases (OMTs; S-adenosyl-L-methionine:o-diphenol O-methyltransferases; EC 2.1.1.6). Here we report on the cloning and the expression pattern of the class I OMT that is specifically involved in lignin biosynthesis. Near-full-length cDNAs have been isolated from tobacco libraries constructed from leaf and stem poly(A)+ RNA. Sequence analysis demonstrated that the OMT I clones derived from two different mRNA species. The two types of OMT I mRNA were reverse transcribed from total RNA and the cDNAs were amplified by polymerase chain reaction and characterized by restriction analysis. The same proportion of the two transcripts was measured in stem tissue of healthy plants and in leaves reacting hypersensitively to tobacco mosaic virus, indicating a coordinate expression of the two OMT I genes. Consistently, genomic hybridization indicated the presence of two OMT I genes in the amphidiploid genome of tobacco. The pattern of expression of OMT I genes was studied by in situ mRNA hybridization. In stem, petiole, and root tissues, OMT I genes were found to be specifically expressed in vascular cells and epidermis. In healthy leaves OMT I mRNA was only detected in vascular strands, whereas, in leaves bearing tobacco mosaic virus-induced necrotic lesions, a particularly strong accumulation of the labeling was also localized in the upper and lower epidermis.

Amino Acid Sequence↗
PubMed1987

In vivo uncoating and efficient expression of foreign mRNAs packaged in TMV-like particles.

The ribonucleocapsids of many plant viruses are extremely stable. The protein coat protects the RNA genome against degradation during the accumulation and spread of progeny virions. Chimeric single-stranded RNA molecules were transcribed in vitro from recombinant plasmids and later encapsidated, in vitro, into ribonucleoprotein particles (pseudoviruses) 60 nanometers long that resembled tobacco mosaic virus. Transcripts encoding an assayable enzyme, chloramphenicol acetyltransferase (CAT), were packaged into pseudovirus particles to assess the utility of this single-stranded RNA delivery system in a wide range of cell types. In all cases, packaged CAT messenger RNA was uncoated and transiently expressed. Significantly higher levels of CAT activity were detected with packaged than with naked CAT messenger RNA after inoculation of plant protoplasts in the presence of polyethylene glycol or abrasive inoculation of intact leaf surfaces. Structural events that lead to the uncoating and expression of CAT messenger RNA showed no cell specificity. This observation may support the view that the comparatively restricted host range of a true plant virus results from events that occur later during the infection cycle.

Acetyltransferases↗