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J. Biol. Chem., Vol. 275, Issue 21, 15969-15976, May 26, 2000
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From 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 antibody 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 spectrometry as NAP-1 and NAP-2,
two members of the nucleosome 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 substrates of an
ATP-dependent glutamylation enzyme co-purifying on the same
column. We took advantage of this property to specifically label and
purify the polyglutamylated 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 glutamylation 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 perspectives for
studying NAP function.
Polyglutamylation of Nucleosome Assembly Proteins*
§,,
Biochimie Cellulaire, Collège de France,
11 place Marcelin Berthelot, 75005 Paris and ¶ Biochimie et
Structure des Protéines, Institut National de la Recherche
Agronomique, 78352 Jouy en Josas Cedex, France
*
This work was supported in part by the Association pour la
Recherche contre le Cancer.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
33-1-44-27-13-07; Fax: 33-1-44-27-13-09; E-mail:
edde@ext.jussieu.fr.
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