title: Cloning and sequencing of a cDNA encoding a heat-stable sweet protein, mabinlin II.
abstract: A cDNA clone encoding a heat-stable sweet protein, mabinlin II (MAB), was isolated and sequenced. The encoded precursor to MAB was composed of 155 amino acid (aa) residues, including a signal sequence of 20 aa, an N-terminal extension peptide of 15 aa, a linker peptide of 14 aa and one residue of C-terminal extension. Comparison of the proteolytic cleavage sites during post-translational processing of MAB precursor with those of like 2S seed-storage proteins of Arabidopsis thaliana, Brassica napus and Bertholletia excelsa shows that the three individual cleavage sites between respective species are conserved.
authors.affiliation: Department of Chemistry, Faculty of Education, Yokohama National University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Nirasawa
authors.forename: Y
authors.initials: Y
authors.lastname: Masuda
authors.forename: K
authors.initials: K
authors.lastname: Nakaya
authors.forename: Y
authors.initials: Y
authors.lastname: Kurihara
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D018076:DNA, Complementary; D018744:DNA, Plant; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics*; D011498:Protein Precursors / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013549:Sweetening Agents
chemical_list: D018076:DNA, Complementary; D018744:DNA, Plant; D010940:Plant Proteins; D011498:Protein Precursors; D013549:Sweetening Agents; C083584:mabinlin protein, Capparis masaikai