Cloning and sequencing of a cDNA encoding a heat-stable sweet protein, mabinlin II

Gene
S NirasawaY Kurihara

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.

References

May 25, 1975·Journal of Molecular Biology·F Sanger, A R Coulson
Jun 11, 1986·Nucleic Acids Research·G von Heijne
Feb 15, 1972·Biochemistry·G BrawermanS Y Lee
Oct 6, 1993·Biochimica Et Biophysica Acta·S NirasawaY Kurihara

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Citations

Aug 26, 1998·Biopolymers·M Kohmura, Y Ariyoshi
Dec 26, 2006·Journal of Bioscience and Bioengineering·Tetsuya Masuda, Naofumi Kitabatake
Feb 5, 2015·World Journal of Microbiology & Biotechnology·Wenliang GuXinwen Hu

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