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J Biol Chem, Vol. 273, Issue 30, 19025-19029, July 24, 1998
From the Nucleolin is one of the major nonribosomal
proteins of the nucleolus. Through its four RNA-binding domains,
nucleolin interacts specifically with pre-rRNA as soon as synthesis
begins, but it is not found in mature cytoplasmic ribosomes. Nucleolin
is able to shuttle between the cytoplasm and the nucleus. These data
suggest that nucleolin might be involved in the nucleolar import of
cytoplasmic components and in the assembly of pre-ribosomal particles.
Here we show, using two-dimensional blots in a ligand blotting assay, that nucleolin interacts with 18 ribosomal proteins from rat (14 and 4 from the large and small subunit, respectively). The C-terminal domain
of nucleolin (p50) interacts with 10 of these identified ribosomal
proteins. In vitro binding assays show that the
glycine-arginine rich domain of nucleolin (RGG domain) is sufficient
for the interaction with one of these proteins. Interestingly, most of
the proteins that interact with p50 belong to the core ribosomal
proteins, which are resistant to extraction with high salt
concentration. These findings suggest that nucleolin might be involved
in the nucleolar targeting of some ribosomal proteins and in their
assembly within pre-ribosomal particles.
Nucleolin Interacts with Several Ribosomal Proteins through
Its RGG Domain
,
Laboratoire de Biologie Moléculaire
Eucaryote, Institut de Biologie Cellulaire et de Génétique
du CNRS, UPR 9006, 118 route de Narbonne, 31062 Toulouse Cedex, France
and ¶ Immuno-Virologie Moléculaire et Cellulaire CNRS
UMR5537, Faculté de Médecine Lyon-R.T.H. Laennec, Rue
Guillaume Paradin, 69372 Lyon Cedex 08, France
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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