Improved bile acid-binding ability of soybean glycinin A1a polypeptide by the introduction of a bile acid-binding peptide (VAWWMY).
We have previously identified a potential bile acid-binding peptide sequence (VAWWMY) in acidic polypeptide A1a of the soybean glycinin A1aB1b subunit (Choi, S. K., et al., Biosci. Biotechnol. Biochem., 66, 2395-2401 (2002)). In this study, we introduced the nucleotide sequence encoding this peptide in the coding DNA which corresponds to amino acids between 251 and 256, and 282 and 287 into the A1a polypeptide by replacement to respectively give modified versions A1aM1 and A1aM2. A fluorescence analysis demonstrates that their bile acid-binding ability was improved compared to A1a. Moreover, modified proglycinin A1aB1b with the VAWWMY sequence at the same sites as those of A1aM1 and A1aM2 was judged to assume the correct conformation. These results suggest the possibility of developing transgenic crops to accumulate the modified glycinin.
Choi
Seon-kang
SK
Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Uji, Japan.
Adachi
Motoyasu
M
Utsumi
Shigeru
S
D000595:Amino Acid Sequence; D001647:Bile Acids and Salts / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D004044:Dietary Proteins; D005916:Globulins / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000235:genetics; D009842:Oligopeptides / Q000737:chemistry; D010940:Plant Proteins / Q000235:genetics; D011485:Protein Binding; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D030262:Soybean Proteins; D013025:Glycine max / Q000737:chemistry*
D001647:Bile Acids and Salts; D002352:Carrier Proteins; D004044:Dietary Proteins; D005916:Globulins; D008562:Membrane Glycoproteins; D009842:Oligopeptides; D010940:Plant Proteins; D030262:Soybean Proteins; C037643:bile acid binding proteins; C011474:glycinin