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Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing.
J Mol Biol. 2005 Feb 18; 346(2):437-55.JM

Abstract

In eukaryotes, pre-rRNA processing depends on cis-acting elements and on a large number of non-ribosomal trans-acting factors, including endonucleases and exonucleases, RNA helicases, rRNA modifying enzymes and components of snoRNPs. The exosome is a conserved eukaryotic protein complex containing multiple 3'-5' exonucleases, which has been implicated in pre-rRNA, snoRNA and snRNA processing, as well as in mRNA degradation. In order to identify new proteins involved in rRNA processing, we have screened a yeast two-hybrid cDNA library, to isolate proteins interacting with the exosome subunit Rrp43p. In this screen, a novel nucleolar protein, Nop17p, was identified which also interacts with the box C/D snoRNP protein Nop58p. The NOP17 gene is not essential for cell viability but its deletion causes a temperature-sensitive phenotype. Pre-rRNA processing analyses revealed that rRNA formation is affected in the Deltanop17 strain subjected to the non-permissive temperature, although it is not blocked completely. In addition, primer extension analyses of RNA isolated from Nop17p-depleted cells subjected to the non-permissive temperature indicates that the pre-rRNA is undergoing different modification or degradation processes in these cells as compared to the parental strain. Nop17p was recently described in the same complex as Nop58p and, interestingly, its depletion leads to mislocalization of Nop1p, Nop56p, Nop58p and Snu13p, which are the core proteins of the box C/D ribonucleoprotein (snoRNP), indicating that Nop17p function is required either for nucleolar retention or for the proper assembly of the box C/D snoRNP.

Authors+Show Affiliations

Department of Biochemistry, Chemistry Institute, USP, São Paulo, SP, Brazil.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15670595

Citation

Gonzales, Fernando A., et al. "Characterization of Saccharomyces Cerevisiae Nop17p, a Novel Nop58p-interacting Protein That Is Involved in Pre-rRNA Processing." Journal of Molecular Biology, vol. 346, no. 2, 2005, pp. 437-55.
Gonzales FA, Zanchin NI, Luz JS, et al. Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J Mol Biol. 2005;346(2):437-55.
Gonzales, F. A., Zanchin, N. I., Luz, J. S., & Oliveira, C. C. (2005). Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. Journal of Molecular Biology, 346(2), 437-55.
Gonzales FA, et al. Characterization of Saccharomyces Cerevisiae Nop17p, a Novel Nop58p-interacting Protein That Is Involved in Pre-rRNA Processing. J Mol Biol. 2005 Feb 18;346(2):437-55. PubMed PMID: 15670595.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. AU - Gonzales,Fernando A, AU - Zanchin,Nilson I T, AU - Luz,Juliana S, AU - Oliveira,Carla C, Y1 - 2004/12/21/ PY - 2004/08/25/received PY - 2004/11/27/revised PY - 2004/11/29/accepted PY - 2005/1/27/pubmed PY - 2005/3/19/medline PY - 2005/1/27/entrez SP - 437 EP - 55 JF - Journal of molecular biology JO - J Mol Biol VL - 346 IS - 2 N2 - In eukaryotes, pre-rRNA processing depends on cis-acting elements and on a large number of non-ribosomal trans-acting factors, including endonucleases and exonucleases, RNA helicases, rRNA modifying enzymes and components of snoRNPs. The exosome is a conserved eukaryotic protein complex containing multiple 3'-5' exonucleases, which has been implicated in pre-rRNA, snoRNA and snRNA processing, as well as in mRNA degradation. In order to identify new proteins involved in rRNA processing, we have screened a yeast two-hybrid cDNA library, to isolate proteins interacting with the exosome subunit Rrp43p. In this screen, a novel nucleolar protein, Nop17p, was identified which also interacts with the box C/D snoRNP protein Nop58p. The NOP17 gene is not essential for cell viability but its deletion causes a temperature-sensitive phenotype. Pre-rRNA processing analyses revealed that rRNA formation is affected in the Deltanop17 strain subjected to the non-permissive temperature, although it is not blocked completely. In addition, primer extension analyses of RNA isolated from Nop17p-depleted cells subjected to the non-permissive temperature indicates that the pre-rRNA is undergoing different modification or degradation processes in these cells as compared to the parental strain. Nop17p was recently described in the same complex as Nop58p and, interestingly, its depletion leads to mislocalization of Nop1p, Nop56p, Nop58p and Snu13p, which are the core proteins of the box C/D ribonucleoprotein (snoRNP), indicating that Nop17p function is required either for nucleolar retention or for the proper assembly of the box C/D snoRNP. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/15670595/Characterization_of_Saccharomyces_cerevisiae_Nop17p_a_novel_Nop58p_interacting_protein_that_is_involved_in_Pre_rRNA_processing_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(04)01552-9 DB - PRIME DP - Unbound Medicine ER -