Identification of a segment of the small nucleolar ribonucleoprotein-associated protein GAR1 that is sufficient for nucleolar accumulation.

Détails

ID Serval
serval:BIB_409CA38D9F3B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Identification of a segment of the small nucleolar ribonucleoprotein-associated protein GAR1 that is sufficient for nucleolar accumulation.
Périodique
The Journal of biological chemistry
Auteur(s)
Girard J.P., Bagni C., Caizergues-Ferrer M., Amalric F., Lapeyre B.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
15/07/1994
Volume
269
Numéro
28
Pages
18499-18506
Langue
anglais
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
GAR1 is a 25-kDa nucleolar protein that is essential for yeast cell growth. The protein is associated with a subset of small nucleolar RNAs and is required for pre-rRNA processing. By expressing in yeast various deletions of GAR1 fused to a reporter protein, we have searched for which particular domain of GAR1 can account for its nucleolar localization. We report here that the glycine/arginine-rich domains of GAR1, which are shared by several other nucleolar proteins, are neither sufficient nor required for the steady-state accumulation of the fusion protein in the nucleolus. We further demonstrate that the central domain of GAR1 is both sufficient to target the beta-galactosidase to the yeast nucleolus and to restore the growth of a strain deficient in GAR1. As opposed to the other characterized nucleolar proteins, the nucleolar targeting domain of GAR1 does not exhibit any homology with the SV40 T-antigen-type nuclear localization sequence. Moreover, none of the modified GAR1 proteins that we examined has allowed us to distinguish the nuclear and nucleolar targeting domains. The presence in GAR1 of a single domain that is responsible for both nuclear entry and nucleolar accumulation suggests that GAR1 either could be carried piggyback by another nucleolar component, possibly as part of a small nucleolar ribonucleoprotein particle, or could be transported to the nucleolus by using a pathway different from the other nucleolar proteins.

Mots-clé
Amino Acid Sequence, Base Sequence, Cell Nucleolus/metabolism, DNA Primers, Escherichia coli/enzymology, Fungal Proteins/biosynthesis, Fungal Proteins/chemistry, Fungal Proteins/metabolism, Genes, Fungal, Molecular Sequence Data, Nuclear Proteins/biosynthesis, Nuclear Proteins/chemistry, Nuclear Proteins/metabolism, Peptide Fragments/chemistry, Peptide Fragments/metabolism, Plasmids, Polymerase Chain Reaction, Recombinant Fusion Proteins/biosynthesis, Recombinant Fusion Proteins/chemistry, Recombinant Fusion Proteins/metabolism, Ribonucleoproteins, Small Nuclear/biosynthesis, Ribonucleoproteins, Small Nuclear/chemistry, Ribonucleoproteins, Small Nuclear/metabolism, Ribonucleoproteins, Small Nucleolar, Saccharomyces cerevisiae/genetics, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins, Schizosaccharomyces/genetics, Sequence Homology, Amino Acid, beta-Galactosidase/biosynthesis
Pubmed
Création de la notice
06/03/2017 18:23
Dernière modification de la notice
03/03/2018 16:29
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