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SUMMARYThe complete nucleotide sequence of the genomic RNA of the potyvirus potato virus Y strain N (PVYn) was obtained from cloned cDNAs. This sequence is 9704 nucleotides long and can encode a polyprotein of 3063 amino acids. The positions of the cleavage sites at the N terminus of the capsid and cytoplasmic inclusion proteins have been determined. Other putative protein cleavage sites have been deduced by searching for consensus sequences and by analogy with the polyprotein of the tobacco vein mottling virus and of the tobacco etch virus. Comparison of the PVY polyprotein sequence with that of other potyvirus polyproteins shows similarities in genome organization and a high level of identity along most of the polyprotein, except for the putative proteins flanking the helper component. A search for specific protein motifs has revealed the existence of a potential metal-binding site at the putative N terminus of the helper component in potyviruses. The possible functions of this structure are discussed.

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We have studied two lines of sunflower (Helianthus annuus L.) selected in the field as drought-tolerant (R1 genotype) or drought-sensitive (S1 genotype). When subjected to drought conditions, the R1 line was able to maintain high leaf water potential longer and wilted later than the S1 line. Therefore, this indicates that R1 tolerance includes a leaf-adaptive response. By subtractive hybridization, we have isolated six different cDNAs (designated sdi for sunflower drought-induced) corresponding to transcripts accumulated in R1 and S1 leaves during adaptive response. Analysis of transcript accumulation in response to drought in both genotypes suggests a preferential expression of three sdi genes in the tolerant line. Abscisic acid-mediated induction, analysed in R1 leaves, was observed for only four sdi genes. Sequence analysis of six sdi clones revealed that five clones were related to known proteins including non specific lipid transfer proteins (nsLTP), early light-induced proteins (ELIP), l-aminocyclopropane-l-carboxylate oxidase (ACC oxidase) or dehydrins, predicted to be involved in a wide range of physiological processes.