Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds

Detalhes bibliográficos
Autor(a) principal: José,Anderson Cleiton
Data de Publicação: 2011
Outros Autores: Silva,Edvaldo Aparecido Amaral da, Davide,Antonio Claudio, Toorop,Peter
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300006
Resumo: The effect of seed drying and imbibition was studied by differential protein expression using two dimensional gel electrophoresis. After drying to a range of water contents, seeds were germinated to assess the viability. Seeds of Magnolia ovata did not withstand the desiccation down to 0.10 g H2O · g-1 dw. The critical water content below which the desiccation sensitivity became apparent was around 0.18 g H2O · g-1 dw (-26.5 MPa). Total protein was extracted and separated by 2D electrophoresis from fresh seeds (0.28 g H2O · g-1 dw), mild dried seeds (0.25 g H2O · g-1 dw) and seeds at low water content (0.10 g H2O · g-1 dw) before and after imbibition for 10 days. The proteome profile revealed the presence of 588 spots on each silver stained gel, from which 21 showed differential expression, correlated with desiccation and germination, by increased or decreased expression. After MS/MS sequencing, three protein spots produced spectra that matched to a Magnolia salicifolia legumin precursor. Results suggested an involvement of this protein in the events taking place during the drying and subsequent imbibitions of the dried seeds.
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spelling Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seedsdesiccation toleranceforest seedleguminproteomicsThe effect of seed drying and imbibition was studied by differential protein expression using two dimensional gel electrophoresis. After drying to a range of water contents, seeds were germinated to assess the viability. Seeds of Magnolia ovata did not withstand the desiccation down to 0.10 g H2O · g-1 dw. The critical water content below which the desiccation sensitivity became apparent was around 0.18 g H2O · g-1 dw (-26.5 MPa). Total protein was extracted and separated by 2D electrophoresis from fresh seeds (0.28 g H2O · g-1 dw), mild dried seeds (0.25 g H2O · g-1 dw) and seeds at low water content (0.10 g H2O · g-1 dw) before and after imbibition for 10 days. The proteome profile revealed the presence of 588 spots on each silver stained gel, from which 21 showed differential expression, correlated with desiccation and germination, by increased or decreased expression. After MS/MS sequencing, three protein spots produced spectra that matched to a Magnolia salicifolia legumin precursor. Results suggested an involvement of this protein in the events taking place during the drying and subsequent imbibitions of the dried seeds.Instituto de Tecnologia do Paraná - Tecpar2011-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300006Brazilian Archives of Biology and Technology v.54 n.3 2011reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132011000300006info:eu-repo/semantics/openAccessJosé,Anderson CleitonSilva,Edvaldo Aparecido Amaral daDavide,Antonio ClaudioToorop,Petereng2011-06-13T00:00:00Zoai:scielo:S1516-89132011000300006Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2011-06-13T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
title Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
spellingShingle Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
José,Anderson Cleiton
desiccation tolerance
forest seed
legumin
proteomics
title_short Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
title_full Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
title_fullStr Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
title_full_unstemmed Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
title_sort Protein expression upon desiccation and imbibition of Magnolia ovata A. St.-Hil seeds
author José,Anderson Cleiton
author_facet José,Anderson Cleiton
Silva,Edvaldo Aparecido Amaral da
Davide,Antonio Claudio
Toorop,Peter
author_role author
author2 Silva,Edvaldo Aparecido Amaral da
Davide,Antonio Claudio
Toorop,Peter
author2_role author
author
author
dc.contributor.author.fl_str_mv José,Anderson Cleiton
Silva,Edvaldo Aparecido Amaral da
Davide,Antonio Claudio
Toorop,Peter
dc.subject.por.fl_str_mv desiccation tolerance
forest seed
legumin
proteomics
topic desiccation tolerance
forest seed
legumin
proteomics
description The effect of seed drying and imbibition was studied by differential protein expression using two dimensional gel electrophoresis. After drying to a range of water contents, seeds were germinated to assess the viability. Seeds of Magnolia ovata did not withstand the desiccation down to 0.10 g H2O · g-1 dw. The critical water content below which the desiccation sensitivity became apparent was around 0.18 g H2O · g-1 dw (-26.5 MPa). Total protein was extracted and separated by 2D electrophoresis from fresh seeds (0.28 g H2O · g-1 dw), mild dried seeds (0.25 g H2O · g-1 dw) and seeds at low water content (0.10 g H2O · g-1 dw) before and after imbibition for 10 days. The proteome profile revealed the presence of 588 spots on each silver stained gel, from which 21 showed differential expression, correlated with desiccation and germination, by increased or decreased expression. After MS/MS sequencing, three protein spots produced spectra that matched to a Magnolia salicifolia legumin precursor. Results suggested an involvement of this protein in the events taking place during the drying and subsequent imbibitions of the dried seeds.
publishDate 2011
dc.date.none.fl_str_mv 2011-06-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300006
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300006
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-89132011000300006
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.54 n.3 2011
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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