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Signal peptide homology between the sweet protein thaumatin II and unrelated cereal α‐amylase/trypsin inhibitors
Author(s) -
Lázaro Ana,
Rodriguez-Palenzuela Pablo,
Maraña Carmen,
Carbonero Pilar,
Garcia-Olmedo Francisco
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80562-3
Subject(s) - thaumatin , signal peptide , biochemistry , trypsin , biology , endosperm , homology (biology) , peptide sequence , complementary dna , nucleic acid sequence , microbiology and biotechnology , chemistry , enzyme , amino acid , gene
A cDNA clone (pUP‐23) corresponding to a member of a protein family that includes inhibitors of trypsin and of heterologous α‐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.