PMID: 15388979Sep 25, 2004Paper

Soybean glycinin A1aB1b subunit has a molecular chaperone-like function to assist folding of the other subunit having low folding ability

Bioscience, Biotechnology, and Biochemistry
Seon-Kang ChoiShigeru Utsumi

Abstract

Soybean (Glycine max L.) glycinin is composed of five subunits which are classified into two groups (group I: A1aB1b, A1bB2, and A2B1a; group II: A3B4 and A5A4B3). All the common soybean cultivars contain both group I and II subunits (Maruyama, N. et al., Phytochemistry, 64, 701-708 (2003)). The biosynthesis of group I starts earlier compared with that of the A3B4 subunit during seed development (Meinke, D.W. et al., Planta, 153, 130-139 (1981)). We have revealed that group I A1aB1b was mostly expressed as a soluble protein, but that A3B4 was expressed mainly as an insoluble protein in Escherichia coli under the same expression conditions; namely, A1aB1b had higher folding ability than A3B4. We therefore assumed that A1aB1b assists folding of group II subunits like a molecular chaperone does. In order to ascertain this, A1aB1b and A3B4 were co-expressed in E. coli. All of the expressed proteins of A3B4 were recovered in a soluble fraction. To confirm this result, we also co-expressed A1aB1b with modified A3B4 versions having extremely low folding ability. All expressed modified A3B4 versions were soluble. These results clearly suggest that A1aB1b has a molecular chaperone-like function in their folding.

References

Apr 1, 1989·The Plant Cell·C D DickinsonN C Nielsen
Jan 16, 1995·FEBS Letters·T YoshizawaK Suzuki
Apr 18, 1994·FEBS Letters·H SorimachiK Suzuki
Dec 23, 2000·Journal of Molecular Biology·M AdachiS Utsumi
Aug 7, 2002·Bioscience, Biotechnology, and Biochemistry·Yuko YamadaMasaaki Yoshikawa
Jan 1, 2003·Bioscience, Biotechnology, and Biochemistry·Seon-Kang ChoiShigeru Utsumi
May 29, 2003·Proceedings of the National Academy of Sciences of the United States of America·Motoyasu AdachiShigeru Utsumi

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