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| Registros recuperados : 2 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Milho e Sorgo. |
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Data corrente: |
14/11/1997 |
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Data da última atualização: |
11/06/2018 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
FONTES, E. P. B.; SILVA, C. J.; CAROLINO, S. M. B.; FIGUEREDO, J. D. F.; BATISTA, D. P. O. |
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Afiliação: |
EMBRAPA/CNPMS. |
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Título: |
A soybean binding protein (BiP) homolog is temporally regulated in soybean seeds and associates detectably with normal storage proteins in vitro. |
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Ano de publicação: |
1996 |
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Fonte/Imprenta: |
Brazilian Journal of Genetics, Ribeirão Preto, v. 19, n. 2, p. 305-312, 1996. |
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Idioma: |
Inglês |
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Conteúdo: |
The endoplasmic reticulum (ER) luminal binding protein (BiP) is thought to be a key mediator of folding and assembly of de novo synthesized secretory proteins. We have used a maize (Zea mays L.) BiP antibady to identify its homolog in soybeans (Glycine max (L.) Merril). The accumulation of BiP in developing soybean seeds seems to be coordinated with the onset of active storage protein synthesis. We used a co-immunoprecipitation assay to detect soybean BiP:B-conglycinin interactions. Either a maize BiP antibody or a-B-conglycinin antibody co-immunoprecipitated the reciprocal protein from whole seed protein extract enzymatically depleted of adenosine 5-triphosphate (ATP), while an unrelated antibody failed to immunoprecipitate either one. The association ofBiP:B-conglycinin complexes was completely reversed by addition of ATP, a diagnostic feature of molecular chaperone-mediated interaction. However, only a very small fraction of B-conglycinin was found to be associated with BiP in whole cell protein extracts from immature seeds. These results are consistent with a transient association between BiP and B-conglycinin subunits, and suggests its involvement in the biosynthetic transport pathway of storage proteins to protein bodies. |
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Palavras-Chave: |
Protein; Seed; Soybean. |
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Thesagro: |
Biologia Molecular; Glycine Max; Proteína; Semente; Soja. |
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Thesaurus NAL: |
molecular biology. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/38228/1/Soybean-binding.pdf
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Marc: |
LEADER 02091naa a2200277 a 4500
001 1477302
005 2018-06-11
008 1996 bl uuuu u00u1 u #d
100 1 $aFONTES, E. P. B.
245 $aA soybean binding protein (BiP) homolog is temporally regulated in soybean seeds and associates detectably with normal storage proteins in vitro.$h[electronic resource]
260 $c1996
520 $aThe endoplasmic reticulum (ER) luminal binding protein (BiP) is thought to be a key mediator of folding and assembly of de novo synthesized secretory proteins. We have used a maize (Zea mays L.) BiP antibady to identify its homolog in soybeans (Glycine max (L.) Merril). The accumulation of BiP in developing soybean seeds seems to be coordinated with the onset of active storage protein synthesis. We used a co-immunoprecipitation assay to detect soybean BiP:B-conglycinin interactions. Either a maize BiP antibody or a-B-conglycinin antibody co-immunoprecipitated the reciprocal protein from whole seed protein extract enzymatically depleted of adenosine 5-triphosphate (ATP), while an unrelated antibody failed to immunoprecipitate either one. The association ofBiP:B-conglycinin complexes was completely reversed by addition of ATP, a diagnostic feature of molecular chaperone-mediated interaction. However, only a very small fraction of B-conglycinin was found to be associated with BiP in whole cell protein extracts from immature seeds. These results are consistent with a transient association between BiP and B-conglycinin subunits, and suggests its involvement in the biosynthetic transport pathway of storage proteins to protein bodies.
650 $amolecular biology
650 $aBiologia Molecular
650 $aGlycine Max
650 $aProteína
650 $aSemente
650 $aSoja
653 $aProtein
653 $aSeed
653 $aSoybean
700 1 $aSILVA, C. J.
700 1 $aCAROLINO, S. M. B.
700 1 $aFIGUEREDO, J. D. F.
700 1 $aBATISTA, D. P. O.
773 $tBrazilian Journal of Genetics, Ribeirão Preto$gv. 19, n. 2, p. 305-312, 1996.
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Registro original: |
Embrapa Milho e Sorgo (CNPMS) |
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