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Tomato contains homologues of Arabidopsis cryptochromes 1 and 2

TitleTomato contains homologues of Arabidopsis cryptochromes 1 and 2
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2000
AuthorsPerrotta, Gaetano, Ninu L., Flamma F., Weller J.L., Kendrick R.E., Nebuloso E., and Giuliano Giovanni
JournalPlant Molecular Biology
KeywordsAmino Acid, Amino Acid Sequence, Arabidopsis, carboxy terminal sequence, chromosomal localization, Chromosome Mapping, Complementary, CRY1 gene, CRY2 gene, Cryptochrome, DNA, DNA repair, Drosophila Proteins, Exons, Eye Proteins, Flavoproteins, G-Protein-Coupled, Gene duplication, gene expression regulation, Genes, genetic conservation, intron, Introns, invertebrate, light, Lycopersicon esculentum, molecular evolution, Molecular Sequence Data, photoreceptor, Photoreceptors, Phylogeny, Plant, Plant Proteins, protein domain, protein expression, Receptors, Sequence Alignment, Sequence Analysis, sequence homology, Tomato

Cryptochromes are blue light photoreceptors found in both plants and animals. They probably evolved from photolyases, which are blue/UV-light-absorbing photoreceptors involved in DNA repair. In seed plants, two different cryptochrome (CRY) genes have been found in Arabidopsis and one in Sinapis, while three genes have been found in the fern Adiantum. We report the characterisation of tomato CRY genes CRY1 and CRY2. They map to chromosomes 4 and 9, respectively, show relatively constitutive expression and encode proteins of 679 and 635 amino acids, respectively. These proteins show higher similarity to their Arabidopsis counterparts than to each other, suggesting that duplication between CRY1 and CRY2 is an ancient event in the evolution of seed plants. The seed plant cryptochromes form a group distinct from the fern cryptochromes, implying that only one gene was present in the common ancestor between these two groups of plants. Most intron positions in CRY genes from plants and ferns are highly conserved. Tomato cry1 and cry2 proteins carry C-terminal domains 210 and 160 amino acids long, respectively. Several conserved motifs are found in these domains, some of which are common to both types of cryptochromes, while others are cryptochrome-type-specific.


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Citation KeyPerrotta2000765