Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a nontypical RNA binding element

Détails

ID Serval
serval:BIB_47AC679969CA
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a nontypical RNA binding element
Périodique
J Biol Chem
Auteur(s)
Bagni C., Lapeyre B.
ISSN
0021-9258 (Print)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
1998
Volume
273
Numéro
18
Pages
10868-73
Notes
Bagni, C
Lapeyre, B
eng
Research Support, Non-U.S. Gov't
1998/06/06
J Biol Chem. 1998 May 1;273(18):10868-73.
Résumé
The nucleolar proteins Gar1p and fibrillarin possess a typical nucleolar glycine/arginine-rich domain and belong to ribonucleoprotein particles. Both proteins are essential for yeast cell growth and are required for pre-rRNA processing. In addition, Gar1p is involved in pre-rRNA pseudouridylation, whereas fibrillarin is required for pre-rRNA methylation. Gar1p and fibrillarin are each associated with a different subset of the small nucleolar RNAs (snoRNAs). Gar1p is co-immunoprecipitated with the H/ACA family of snoRNAs, whereas fibrillarin is co-immunoprecipitated with the C/D family. However, attempts to demonstrate direct interactions between fibrillarin and snoRNAs have failed, and such interactions between Gar1p and the H/ACA snoRNAs had not yet been reported. Among the H/ACA snoRNAs associated with Gar1p, one can distinguish a large group of snoRNAs that are not essential in yeast and serve as guides for pseudouridine synthesis onto the pre-rRNA molecule. In contrast, the two snoRNAs snR10 and snR30 are required for normal cell growth and for pre-rRNA cleavage. We show here that Gar1p interacts in vitro directly and specifically with these two snoRNAs. Deletion analysis of Gar1p indicates that a major RNA binding element, which is extremely well conserved throughout evolution, lies in the middle of the protein. However, this domain alone binds poorly to the target RNAs and an accessory domain is required to restore efficient binding. The accessory domain can be either one of the glycine/arginine-rich domains or a second element of the core of the protein that is highly conserved between different species.
Mots-clé
Amino Acid Sequence, Fungal Proteins/chemistry/*metabolism, Molecular Sequence Data, Nuclear Proteins/chemistry/*metabolism, Protein Binding, RNA, Small Nuclear/*metabolism, RNA-Binding Proteins/*metabolism, *Ribonucleoproteins, Small Nucleolar, Saccharomyces cerevisiae/genetics/metabolism, *Saccharomyces cerevisiae Proteins, Sequence Deletion, Sequence Homology, Amino Acid
Pubmed
Création de la notice
06/03/2017 18:23
Dernière modification de la notice
03/03/2018 16:50
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