FEBS Letters · 1988 · 24 citations · 16 references
Life SciencesBiochemistryPlant BiologyMolecular EvolutionPlant BiochemistryPlant Molecular BiologyAmino Acid Sequence DeterminantsEnzyme InhibitionPlant EnzymesProtein Sequence AnalysisProteolytic EnzymesProteolytic ProcessingCdna CloningCdna Library ConstructionPlant ProteasesProtein Family AnalysisProtein Family EvolutionSignal Peptide AnalysisSignal Peptide MotifThaumatin-like Proteins
A cDNA clone (pUP-23) corresponding to a member of a protein family that includes inhibitors of trypsin and of heterologous alpha-amylases has been selected from a library derived from developing barley endosperm and its sequence has been determined. A stretch of 95 nucleotides that included the signal peptide and the first 8 residues of the mature protein was found to be homologous to an exactly equivalent region of the nucleotide sequence encoding the sweet protein thaumatin II. Evolutionary implications of this finding are discussed.
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