
doi: 10.1007/bf00014451
pmid: 8204834
A clone obtained from a broad bean (Vicia faba) developing cotyledon cDNA library contained the complete coding sequence of a polypeptide with very high homology to the small GTP-binding proteins Ran from human cells and Spi1 from yeast. These proteins belong to the ras superfamily of proteins involved in different basic cellular processes. The Ran/Spi1 proteins interact with a protein bound to DNA (RCC1) and are thought to function in the regulation of the cell cycle. The amino acid sequence of the obtained plant Ran-homologue, designated Vfa-ran, is 74% and 76% identical to Ran and Spi1, respectively. The five functional, conserved domains of ras-related proteins are present in the Vfa-ran sequence. However, as in Ran/Spi1 the C-terminus of Vfa-ran is very acidic and lacks the Cys motif for isoprenylation. Northern blotting revealed a corresponding mRNA expression in broad bean roots, leaves, and cotyledons with the highest level in roots.
DNA, Complementary, Plants, Medicinal, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Fabaceae, ran GTP-Binding Protein, GTP-Binding Proteins, Amino Acid Sequence, Conserved Sequence, Plant Proteins
DNA, Complementary, Plants, Medicinal, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Fabaceae, ran GTP-Binding Protein, GTP-Binding Proteins, Amino Acid Sequence, Conserved Sequence, Plant Proteins
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