Cargando…
α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds*
The α′ and β subunits of soybean β-conglycinin were expressed in rice seeds in order to improve the nutritional and physiological properties of rice as a food. The α′ subunit accumulated in rice seeds at a higher level than the β subunit, but no detectable difference in mRNA transcription level betw...
Autores principales: | , , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755024/ https://www.ncbi.nlm.nih.gov/pubmed/19656819 http://dx.doi.org/10.1093/jxb/erp235 |
_version_ | 1782172428837847040 |
---|---|
author | Motoyama, Takayasu Maruyama, Nobuyuki Amari, Yoshiki Kobayashi, Kanna Washida, Haruhiko Higasa, Takahiko Takaiwa, Fumio Utsumi, Shigeru |
author_facet | Motoyama, Takayasu Maruyama, Nobuyuki Amari, Yoshiki Kobayashi, Kanna Washida, Haruhiko Higasa, Takahiko Takaiwa, Fumio Utsumi, Shigeru |
author_sort | Motoyama, Takayasu |
collection | PubMed |
description | The α′ and β subunits of soybean β-conglycinin were expressed in rice seeds in order to improve the nutritional and physiological properties of rice as a food. The α′ subunit accumulated in rice seeds at a higher level than the β subunit, but no detectable difference in mRNA transcription level between subunits was observed. Sequential extraction results indicate that the α′ subunit formed one or more disulphide bonds with glutelin. Electron microscopic analysis showed that the α′ subunit and the β subunit were transported to PB-II together with glutelin. In mature transgenic seeds, the β subunit accumulated in low electron density regions in the periphery of PB-II, whereas the α′ subunit accumulated together with glutelin in high-density regions of the periphery. The subcellular localization of mutated α′ subunits lacking one cysteine residue in the N-terminal mature region (α′ΔCys1) or five cysteine residues in the pro and N-terminal mature regions (α′ΔCys5) were also examined. Low-density regions were formed in PB-II in mature seeds of transgenic rice expressing α′ΔCys 5 and α′ΔCys1. α′ΔCys5 was localized only in the low-density regions, whereas α′ΔCys1 was found in both low- and high-density regions. These results suggest that the α′ subunit could make a complex via one or more disulphide bonds with glutelin and accumulate together in PB-II of transgenic rice seeds. |
format | Text |
id | pubmed-2755024 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27550242009-10-02 α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* Motoyama, Takayasu Maruyama, Nobuyuki Amari, Yoshiki Kobayashi, Kanna Washida, Haruhiko Higasa, Takahiko Takaiwa, Fumio Utsumi, Shigeru J Exp Bot Research Papers The α′ and β subunits of soybean β-conglycinin were expressed in rice seeds in order to improve the nutritional and physiological properties of rice as a food. The α′ subunit accumulated in rice seeds at a higher level than the β subunit, but no detectable difference in mRNA transcription level between subunits was observed. Sequential extraction results indicate that the α′ subunit formed one or more disulphide bonds with glutelin. Electron microscopic analysis showed that the α′ subunit and the β subunit were transported to PB-II together with glutelin. In mature transgenic seeds, the β subunit accumulated in low electron density regions in the periphery of PB-II, whereas the α′ subunit accumulated together with glutelin in high-density regions of the periphery. The subcellular localization of mutated α′ subunits lacking one cysteine residue in the N-terminal mature region (α′ΔCys1) or five cysteine residues in the pro and N-terminal mature regions (α′ΔCys5) were also examined. Low-density regions were formed in PB-II in mature seeds of transgenic rice expressing α′ΔCys 5 and α′ΔCys1. α′ΔCys5 was localized only in the low-density regions, whereas α′ΔCys1 was found in both low- and high-density regions. These results suggest that the α′ subunit could make a complex via one or more disulphide bonds with glutelin and accumulate together in PB-II of transgenic rice seeds. Oxford University Press 2009-10 2009-08-05 /pmc/articles/PMC2755024/ /pubmed/19656819 http://dx.doi.org/10.1093/jxb/erp235 Text en © 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
spellingShingle | Research Papers Motoyama, Takayasu Maruyama, Nobuyuki Amari, Yoshiki Kobayashi, Kanna Washida, Haruhiko Higasa, Takahiko Takaiwa, Fumio Utsumi, Shigeru α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* |
title | α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* |
title_full | α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* |
title_fullStr | α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* |
title_full_unstemmed | α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* |
title_short | α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* |
title_sort | α′ subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds* |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755024/ https://www.ncbi.nlm.nih.gov/pubmed/19656819 http://dx.doi.org/10.1093/jxb/erp235 |
work_keys_str_mv | AT motoyamatakayasu asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds AT maruyamanobuyuki asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds AT amariyoshiki asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds AT kobayashikanna asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds AT washidaharuhiko asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds AT higasatakahiko asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds AT takaiwafumio asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds AT utsumishigeru asubunitofsoybeanbconglycininformscomplexwithriceglutelinviaadisulphidebondintransgenicriceseeds |