Proteins associated with cork formation in Quercus suber L. stem tissues
Identifieur interne : 000036 ( PascalFrancis/Corpus ); précédent : 000035; suivant : 000037Proteins associated with cork formation in Quercus suber L. stem tissues
Auteurs : Cândido P. P. Ricardo ; Isabel Martins ; Rita Francisco ; Kjell Sergeant ; Carla Pinheiro ; Alexandre Campos ; Jenny Renaut ; Pedro FevereiroSource :
- Journal of proteomics : (Print) [ 1874-3919 ] ; 2011.
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- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.
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Pour connaître la documentation sur le format Inist Standard.
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Format Inist (serveur)
NO : | PASCAL 11-0407790 INIST |
---|---|
ET : | Proteins associated with cork formation in Quercus suber L. stem tissues |
AU : | RICARDO (Cândido P. P.); MARTINS (Isabel); FRANCISCO (Rita); SERGEANT (Kjell); PINHEIRO (Carla); CAMPOS (Alexandre); RENAUT (Jenny); FEVEREIRO (Pedro); RENAUT (Jenny); SVENSSON (Birte); JORRIN-NOVO (Jesus); PANIS (Bart) |
AF : | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN/2780-157 Oeiras/Portugal (1 aut., 2 aut., 3 aut., 5 aut., 6 aut., 8 aut.); Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Tapada da Ajuda/1349-017 Lisboa/Portugal (1 aut.); Centre de Recherche Public-Gabriel Lippmann, Department Environment and Agrobiotechnologies, 41, rue du Brill/4422 Belvaux/Luxembourg (4 aut., 7 aut.); Faculdade de Ciencias, Universidade de Lisboa, Campo Grande/1749-016 Lisboa/Portugal (8 aut.); Laboratory of Tropical Crop Improvement, Department of Biosystems, K. U. Leuven, Kasteelpark Arenberg 13/3001 Heverlee/Belgique (4 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Journal of proteomics : (Print); ISSN 1874-3919; Royaume-Uni; Da. 2011; Vol. 74; No. 8; Pp. 1266-1278; Bibl. 66 ref. |
LA : | Anglais |
EA : | Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation. |
CC : | 002A04B |
FD : | Protéine; Quercus suber; Tissu; Protéomique |
FG : | Fagaceae; Dicotyledones; Angiospermae; Spermatophyta |
ED : | Protein; Quercus suber; Tissue; Proteomics |
EG : | Fagaceae; Dicotyledones; Angiospermae; Spermatophyta |
SD : | Proteína; Quercus suber; Tejido; Proteómica |
LO : | INIST-18007.354000191153520090 |
ID : | 11-0407790 |
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Pascal:11-0407790Le document en format XML
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<front><div type="abstract" xml:lang="en">Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.</div>
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<fC01 i1="01" l="ENG"><s0>Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A04B</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Protéine</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Protein</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Proteína</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Quercus suber</s0>
<s2>NS</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Quercus suber</s0>
<s2>NS</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Quercus suber</s0>
<s2>NS</s2>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Tissu</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Tissue</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Tejido</s0>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Protéomique</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Proteomics</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Proteómica</s0>
<s5>04</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Fagaceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Fagaceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Fagaceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Dicotyledones</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Dicotyledones</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Dicotyledones</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Angiospermae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Angiospermae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Angiospermae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Spermatophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Spermatophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Spermatophyta</s0>
<s2>NS</s2>
</fC07>
<fN21><s1>283</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
<server><NO>PASCAL 11-0407790 INIST</NO>
<ET>Proteins associated with cork formation in Quercus suber L. stem tissues</ET>
<AU>RICARDO (Cândido P. P.); MARTINS (Isabel); FRANCISCO (Rita); SERGEANT (Kjell); PINHEIRO (Carla); CAMPOS (Alexandre); RENAUT (Jenny); FEVEREIRO (Pedro); RENAUT (Jenny); SVENSSON (Birte); JORRIN-NOVO (Jesus); PANIS (Bart)</AU>
<AF>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN/2780-157 Oeiras/Portugal (1 aut., 2 aut., 3 aut., 5 aut., 6 aut., 8 aut.); Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Tapada da Ajuda/1349-017 Lisboa/Portugal (1 aut.); Centre de Recherche Public-Gabriel Lippmann, Department Environment and Agrobiotechnologies, 41, rue du Brill/4422 Belvaux/Luxembourg (4 aut., 7 aut.); Faculdade de Ciencias, Universidade de Lisboa, Campo Grande/1749-016 Lisboa/Portugal (8 aut.); Laboratory of Tropical Crop Improvement, Department of Biosystems, K. U. Leuven, Kasteelpark Arenberg 13/3001 Heverlee/Belgique (4 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of proteomics : (Print); ISSN 1874-3919; Royaume-Uni; Da. 2011; Vol. 74; No. 8; Pp. 1266-1278; Bibl. 66 ref.</SO>
<LA>Anglais</LA>
<EA>Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.</EA>
<CC>002A04B</CC>
<FD>Protéine; Quercus suber; Tissu; Protéomique</FD>
<FG>Fagaceae; Dicotyledones; Angiospermae; Spermatophyta</FG>
<ED>Protein; Quercus suber; Tissue; Proteomics</ED>
<EG>Fagaceae; Dicotyledones; Angiospermae; Spermatophyta</EG>
<SD>Proteína; Quercus suber; Tejido; Proteómica</SD>
<LO>INIST-18007.354000191153520090</LO>
<ID>11-0407790</ID>
</server>
</inist>
</record>
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