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F Chapeville

Publications and source records attributed to F Chapeville.

At least 19 recordsLinked to original sources

An enigma: the role of viral RNA aminoacylation.

The first demonstration on the aminoacylation capacity of the RNA genome of a plant virus appeared more than 25 years ago. Shortly thereafter, aminoacylation of the RNA genome of a number of other plant viruses was observed. This led to considerable work on the tRNA-like region of these viral RNAs, and to the first demonstration of the presence of pseudoknots in their folding pattern. In spite of the vast amount of efforts put into trying to understand the reason for the aminoacylation capacity of certain viral RNA genomes, as yet no clear general conclusion emerges. It rather looks as though the reason for aminoacylation may be different for different viruses, and that aminoacylation may operate at different levels in the virus life cycle. Given that certain RNA viruses possess structures which resemble that of tRNAs at their 5'- or 3'-termini, it is most likely that convergent evolution may have dominated the appearance of such structures in the virus world.

Amino Acyl-tRNA Synthetases↗

Plant viruses and new perspectives in cross-protection.

Cross-protection in plants is the phenomenon whereby a plant preinoculated with a mild virus strain becomes resistant to subsequent inoculation by a related severe strain. It has been used on a large scale in cases where no resistant plants are available. Although several hypotheses have been proposed to explain the molecular mechanism underlying cross-protection, no single hypothesis can account for all the data obtained. Recently, a phenomenon akin to cross-protection has been achieved in transformed plants harboring the cDNA of a part of a viral RNA genome. These results obtained by genetic engineering raise new hopes for obtaining plants resistant to virus infection.

Genetic Engineering↗

Qualitative and quantitative distribution of plasminogen activators in organs from healthy adult mice.

Twenty organs from healthy adult mice were tested for plasminogen activator activity. All were positive although specific activities varied 200-fold. Tissues with high activity were lung, uterus, brain and kidney. Endocrine glands were moderately rich in activator activity, and lymphoid tissues were poor. Molecular mass characterization was carried out. Two enzymatic forms were observed in all twenty organs: a 70 kDa form similar to human tissue plasminogen activator and a 48 kDa form analogous to mouse urokinase.

Animals↗

Conformational requirements of tobacco mosaic virus RNA for aminoacylation and adenylation.

The RNA conformational requirements for both aminoacylation and adenylation emerging from our studies performed using the valine- and the tyrosine-accepting plant viral RNAs are now strongly supported by the histidine-accepting tobacco mosaic virus RNA: an 'L'-shaped conformation is recognized by the aminoacyl-tRNA synthetase whereas only the aminoacyl RNA domain (equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T stem and loop) interacts with the tRNA nucleotidyltransferase.

Amino Acyl-tRNA Synthetases↗

Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu.

Turnip yellow mosaic virus (TYMV) Val-RNA forms a complex with the peptide elongation factor Tu (EF-Tu) in the presence of GTP: the Val-RNA is protected by EF-Tu.GTP from non-enzymatic deacylation and nuclease digestion. The determination of the length of the shortest TYMV Val-RNA fragment that binds EF-Tu.GTP leads us to conclude that the valylated aminoacyl RNA domain equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T arm is sufficient for complex formation. Since the aminoacyl RNA domain is also sufficient for adenylation by the ATP(CTP):tRNA nucleotidyltransferase, an analogy can be drawn between these two tRNA-specific proteins.

Journal Article↗

tRNA-like structures of plant viral RNAs: conformational requirements for adenylation and aminoacylation.

Bromo- and cucumovirus RNAs contain a tRNA-like structure as an integral part of their genome. This structure is located at the 3' end of the viral RNA and is an acceptor of tyrosine. The 3' regions of representative viral RNAs have been sequenced and quite unorthodox secondary foldings have been proposed for these 3' ends. The question therefore remained as to how these structures could be recognized by tRNA-specific enzymes. We have established the minimum number of nucleotides from the 3' end of the brome mosaic virus and broad bean mottle virus RNAs required for the formation of structures recognized by the tyrosyl-tRNA synthetase and/or the tRNA nucleotidyltransferase. The results obtained delineate the length of the tRNA-like region, and indicate that the 5' region of the tRNA-like structure participates in the formation of the amino acid stem. This has led us to propose an 'L'-shaped secondary structure for these tRNA-like regions.

Anticodon↗

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Genetics↗

Length requirements for tRNA-specific enzymes and cleavage specificity at the 3' end of turnip yellow mosaic virus RNA.

This paper describes the minimum length of the turnip yellow mosaic virus (TYMV) RNA necessary to fulfill the tRNA-like properties of the viral RNA: 50 to 75 nucleotides and 86 nucleotides from the 3' end of TYMV RNA are sufficient for adenylation and valylation respectively by the Escherichia coli system. The size of the tRNA-like fragments obtained in vitro in the presence of an E. coli, a reticulocyte or a chinese cabbage leaf extract has also been determined. Among the major fragments liberated from the 3' end of TYMV RNA by the three systems are fragments of 117 and 112 nucleotides. In addition, the E. coli extract liberates fragments of 139 and 61 nucleotides, and the reticulocyte lysate fragments of 109, 94, 84, 73 and 46 nucleotides. The cleavage of the viral RNA by several systems in vitro to yield RNA fragments encompassing the tRNA-like sequence suggests that such fragments might also be liberated in vivo.

Base Composition↗

Turnip yellow mosaic virus RNA is aminoacylated in vivo in Chinese cabbage leaves.

Turnip yellow mosaic virus (TYMV) contains a tRNA-like structure as an integral part of its genome. This structure is located at the extreme 3' end of the viral RNA and is the acceptor of valine after 3'-terminal adenylation. It is known that in vitro (with bacterial, yeast, or plant systems) and in vivo (upon microinjection into Xenopus laevis oocytes) a series of tRNA-specific enzymes can recognize this structure in the viral RNA. We report that TYMV RNA is valylated and consequently adenylated in vivo in its natural host, Chinese cabbage leaves. This suggests that the acylated form of the viral RNA could play an important role in the life-cycle of the virus.

Journal Article↗