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Titre : Cyclin-dependent kinase (CDK) inhibitors regulate the CDK-cyclin complex activities in endoreduplicating cells of developing tomato fruit Type de document : document électronique Auteurs : Badia Bisbis, Auteur ; Frédéric Delmas, Auteur ; Jerome Joubes, Auteur Editeur : The American Society for Biochemistry and Molecular Biology Année de publication : 2006 Importance : 281 (11) Note générale : VOL. 281, NO. 11, pp. 7374 –7383, Langues : Anglais (eng) Catégories : 575 Anatomie et physiologie végétales Tags : 'CDK CYCLIN DEPENDENT KINASE , INHIBITEUR DE CDK ENDOREDUPLICATION BIOLOGIE VEGETALE FRUIT DEVELOPPEMENT DU FRUIT CYCLE CELLULAIRE '. Index. décimale : 575 Résumé : The jelly-like locular (gel) tissue of tomato fruit is made up of large thin-walled and highly vacuolized cells. The development of the gel tissue is characterized by the arrest of mitotic activities, the inhibition of cyclin-dependent kinase A (CDKA) activity, and numerous rounds of nuclear DNA endoreduplication. To decipher the molecular determinants controlling these developmental events, we investigated the putative involvement of CDK inhibitors (p27 Kip -related proteins, or KRPs) during the endoreduplication process. Two cDNAs, LeKRP1 and LeKRP2, encoding tomato CDK
inhibitors were isolated. The LeKRP1 and LeKRP2 transcript expression was shown to be enhanced in the differentiating cells of the gel undergoing endoreduplication. At the translational level,LeKRP1 was shown to accumulate in the gel tissue and to participate in the inhibition of the CDK-cyclin kinase activities occurring in endoreduplicating cells of the gel tissue. We here propose that LeKRP1 participates in the control of both the cell cycle and the
endoreduplication cycleEn ligne : https://hal.inrae.fr/hal-02661083v1 Format de la ressource électronique : Cyclin-dependent kinase (CDK) inhibitors regulate the CDK-cyclin complex activities in endoreduplicating cells of developing tomato fruit [document électronique] / Badia Bisbis, Auteur ; Frédéric Delmas, Auteur ; Jerome Joubes, Auteur . - The American Society for Biochemistry and Molecular Biology, 2006 . - 281 (11).
VOL. 281, NO. 11, pp. 7374 –7383,
Langues : Anglais (eng)
Catégories : 575 Anatomie et physiologie végétales Tags : 'CDK CYCLIN DEPENDENT KINASE , INHIBITEUR DE CDK ENDOREDUPLICATION BIOLOGIE VEGETALE FRUIT DEVELOPPEMENT DU FRUIT CYCLE CELLULAIRE '. Index. décimale : 575 Résumé : The jelly-like locular (gel) tissue of tomato fruit is made up of large thin-walled and highly vacuolized cells. The development of the gel tissue is characterized by the arrest of mitotic activities, the inhibition of cyclin-dependent kinase A (CDKA) activity, and numerous rounds of nuclear DNA endoreduplication. To decipher the molecular determinants controlling these developmental events, we investigated the putative involvement of CDK inhibitors (p27 Kip -related proteins, or KRPs) during the endoreduplication process. Two cDNAs, LeKRP1 and LeKRP2, encoding tomato CDK
inhibitors were isolated. The LeKRP1 and LeKRP2 transcript expression was shown to be enhanced in the differentiating cells of the gel undergoing endoreduplication. At the translational level,LeKRP1 was shown to accumulate in the gel tissue and to participate in the inhibition of the CDK-cyclin kinase activities occurring in endoreduplicating cells of the gel tissue. We here propose that LeKRP1 participates in the control of both the cell cycle and the
endoreduplication cycleEn ligne : https://hal.inrae.fr/hal-02661083v1 Format de la ressource électronique :
Titre : Polyglutamylation of nucleosome assembly proteins Type de document : document électronique Auteurs : Catherine Regnard, Auteur ; Elisabeth Desbruyères, Auteur ; Jean-Claude Huet, Auteur ; Christian Beauvallet, Auteur ; J Claude Pernollet, Auteur ; Bernard Edde, Auteur Editeur : The American Society for Biochemistry and Molecular Biology Année de publication : 2000 Importance : Vol. 275,, No. 21;pp. 15969 –15976 Format : HTML Accompagnement : ISBN/ISSN/EAN : 1083-351X Langues : Anglais (eng) Catégories : 572 Biochimie Tags : Sciences du Vivant Biochimie Biologie Moléculaire q-bio.BM q-bio Biochimie bactérienne Index. décimale : 572.6 Résumé : Polyglutamylation is an original posttranslational modification, discovered on tubulin, consisting in side chains composed of several glutamyl units and leading to a very unusual protein structure. A monoclonal anti-body directed against glutamylated tubulin (GT335) was found to react with other proteins present in HeLa cells.
After immunopurification on a GT335 affinity column,two prominent proteins of ;50 kDa were observed. They were identified by microsequencing and mass spectrom-etry as NAP-1 and NAP-2, two members of the nucleo-some assembly protein family that are implicated in the deposition of core histone complexes onto chromatin.
Strikingly, NAP-1 and NAP-2 were found to be sub-strates of an ATP-dependent glutamylation enzyme co-purifying on the same column. We took advantage of this property to specifically label and purify the polyglu-tamylated peptides. NAP-1 and NAP-2 are modified in their C-terminal domain by the addition of up to 9 and 10 glutamyl units, respectively. Two putative glutamyla-tion sites were localized for NAP-1 at Glu-356 and Glu-357 and, for NAP-2, at Glu-347 and Glu-348. These results demonstrate for the first time that proteins other than tubulin are polyglutamylated and open new perspec-tives for studying NAP function.
En ligne : https://hal.inrae.fr/hal-02698374 Format de la ressource électronique : HTML Polyglutamylation of nucleosome assembly proteins [document électronique] / Catherine Regnard, Auteur ; Elisabeth Desbruyères, Auteur ; Jean-Claude Huet, Auteur ; Christian Beauvallet, Auteur ; J Claude Pernollet, Auteur ; Bernard Edde, Auteur . - The American Society for Biochemistry and Molecular Biology, 2000 . - Vol. 275,, No. 21;pp. 15969 –15976 ; HTML + PDF.
ISSN : 1083-351X
Langues : Anglais (eng)
Catégories : 572 Biochimie Tags : Sciences du Vivant Biochimie Biologie Moléculaire q-bio.BM q-bio Biochimie bactérienne Index. décimale : 572.6 Résumé : Polyglutamylation is an original posttranslational modification, discovered on tubulin, consisting in side chains composed of several glutamyl units and leading to a very unusual protein structure. A monoclonal anti-body directed against glutamylated tubulin (GT335) was found to react with other proteins present in HeLa cells.
After immunopurification on a GT335 affinity column,two prominent proteins of ;50 kDa were observed. They were identified by microsequencing and mass spectrom-etry as NAP-1 and NAP-2, two members of the nucleo-some assembly protein family that are implicated in the deposition of core histone complexes onto chromatin.
Strikingly, NAP-1 and NAP-2 were found to be sub-strates of an ATP-dependent glutamylation enzyme co-purifying on the same column. We took advantage of this property to specifically label and purify the polyglu-tamylated peptides. NAP-1 and NAP-2 are modified in their C-terminal domain by the addition of up to 9 and 10 glutamyl units, respectively. Two putative glutamyla-tion sites were localized for NAP-1 at Glu-356 and Glu-357 and, for NAP-2, at Glu-347 and Glu-348. These results demonstrate for the first time that proteins other than tubulin are polyglutamylated and open new perspec-tives for studying NAP function.
En ligne : https://hal.inrae.fr/hal-02698374 Format de la ressource électronique : HTML Documents numériques
Polyglutamylation of nucleosome assembly proteinsURL
