Cloning and sequencing of a cDNA encoding a heat-stable sweet protein, mabinlin II.
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.
Nirasawa
S
S
Department of Chemistry, Faculty of Education, Yokohama National University, Japan.
Masuda
Y
Y
Nakaya
K
K
Kurihara
Y
Y
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
D018076:DNA, Complementary; D018744:DNA, Plant; D010940:Plant Proteins; D011498:Protein Precursors; D013549:Sweetening Agents; C083584:mabinlin protein, Capparis masaikai