|
| 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 : |
PDF |
| 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 |
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