Characterization of Saccharomyces cerevisiae Nop17p, a Novel Nop58p-Interacting Protein that is Involved in Pre-rRNA Processing

Gonzales-Zubiate, Fernando A.; Zanchin, Nilson Ivo Tonin; Luz, Juliana Silva da; Oliveira, Carla C.

doi:10.1016/j.jmb.2004.11.071

Cited by 79 publications

(129 citation statements)

References 59 publications

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…Intriguingly, like NAP57, yeast NOP58 interacts with yeast PIH1D1 (Nop17; Gonzales et al 2005). Therefore, pontin and reptin action may generally require highly charged and unstructured amino acid tails.…”

Section: Discussionmentioning

confidence: 99%

Mechanism of the AAA+ ATPases pontin and reptin in the biogenesis of H/ACA RNPs

Machado-Pinilla

Liger

Leulliot

et al. 2012

RNA

View full text Add to dashboard Cite

The AAA+ ATPases pontin and reptin function in a staggering array of cellular processes including chromatin remodeling, transcriptional regulation, DNA damage repair, and assembly of macromolecular complexes, such as RNA polymerase II and small nucleolar (sno) RNPs. However, the molecular mechanism for all of these AAA+ ATPase associated activities is unknown. Here we document that, during the biogenesis of H/ACA RNPs (including telomerase), the assembly factor SHQ1 holds the pseudouridine synthase NAP57/dyskerin in a viselike grip, and that pontin and reptin (as components of the R2TP complex) are required to pry NAP57 from SHQ1. Significantly, the NAP57 domain captured by SHQ1 harbors most mutations underlying X-linked dyskeratosis congenita (X-DC) implicating the interface between the two proteins as a target of this bone marrow failure syndrome. Homing in on the essential first steps of H/ACA RNP biogenesis, our findings provide the first insight into the mechanism of action of pontin and reptin in the assembly of macromolecular complexes.

show abstract

Section: Discussionmentioning

confidence: 99%

Mechanism of the AAA+ ATPases pontin and reptin in the biogenesis of H/ACA RNPs

Machado-Pinilla

Liger

Leulliot

et al. 2012

RNA

View full text Add to dashboard Cite

show abstract

“…Its yeast homologue NOP17p is known to be located in nucleoli where it interacts with snoRNP protein NOP58p, exosome component Prp43p (homologous to mammalian OIP-2) and NOP53p. These proteins are involved in pre-rRNA processing [21].…”

Section: Discussionmentioning

confidence: 99%

Characterization of hampin/MSL1 as a node in the nuclear interactome

Dmitriev

Korneenko

Бессонов

et al. 2007

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Hampin, homolog of drosophila MSL1, is a partner of histone acetyltransferase MYST1/MOF. Functions of these proteins remain poorly understood beyond their participation in chromatin remodeling complex MSL. In order to identify new proteins interacting with hampin, we screened a mouse cDNA library in yeast two-hybrid system with mouse hampin as bait and found five highconfidence interactors: MYST1, TPR proteins TTC4 and KIAA0103, NOP17 (homolog of a yeast nucleolar protein) and transcription factor GC BP. Subsequently, all these proteins were used as baits in library screenings and more new interactions were found: tumor suppressor RASSF1C and spliceosome component PRP3 for KIAA0103, ring finger RNF10 for RASSF1C, and RNA polymerase II regulator NELF-C for MYST1. The majority of the observed interactions was confirmed in vitro by pull-down of bacterially expressed proteins. Reconstruction of a fragment of mammalian interactome suggests that hampin may be linked to diverse regulatory processes in the nucleus.

show abstract

“…In previous studies, it was shown that Rvb2 depletion as well as PIH1 deletion caused delocalization of snoRNP proteins [25,38]. Since Pih1 seems to act as an adaptor between R2TP and Nop58 ( Figure 1C,E), we examined how Pih1 might affect R2TP and snoRNP localizations by observing GFP fusion proteins of all related components in pih1Δ background.…”

Section: Pih1 Is Required For the Proper Localization Of R2tp And Boxmentioning

confidence: 97%

“…Also, Gonzales et al [25] showed a physical interaction between Pih1 and Nop58. However, the detailed molecular basis of R2TP complex function in box C/D snoRNP biogenesis remains unknown.…”

Section: R2tp Interacts With Nop58 Through Pih1mentioning

confidence: 97%

“…Rvb1 and Rvb2 are members of AAA + (ATPase associated with diverse cellular activities) superfamily and, in addition to snoRNP assembly, are involved in many other critical cellular processes such as chromatin remodeling, DNA replication, DNA damage repair, transcription, and telomerase assembly [23,24]. Pih1 (also known as Nop17) was initially isolated as a Nop58 interacting protein in yeast [25] and, subsequently, shown to be part of the R2TP complex and to interact with Hsp90 [14,21]. Tah1 contains two tetratricopeptide repeat (TPR) motifs and acts as a co-factor for Hsp90 to stabilize Pih1 [14,26].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex

et al. 2014

View full text Add to dashboard Cite

Background: Box C/D snoRNPs, which are typically composed of box C/D snoRNA and the four core protein components Nop1, Nop56, Nop58, and Snu13, play an essential role in the modification and processing of pre-ribosomal RNA. The highly conserved R2TP complex, comprising the proteins Rvb1, Rvb2, Tah1, and Pih1, has been shown to be required for box C/D snoRNP biogenesis and assembly; however, the molecular basis of R2TP chaperone-like activity is not yet known. Results: Here, we describe an unexpected finding in which the activity of the R2TP complex is required for Nop58 protein stability and is controlled by the dynamic subcellular redistribution of the complex in response to growth conditions and nutrient availability. In growing cells, the complex localizes to the nucleus and interacts with box C/D snoRNPs. This interaction is significantly reduced in poorly growing cells as R2TP predominantly relocalizes to the cytoplasm. The R2TP-snoRNP interaction is mainly mediated by Pih1. Conclusions:The R2TP complex exerts a novel regulation on box C/D snoRNP biogenesis that affects their assembly and consequently pre-rRNA maturation in response to different growth conditions.

show abstract

Characterization of Saccharomyces cerevisiae Nop17p, a Novel Nop58p-Interacting Protein that is Involved in Pre-rRNA Processing

Cited by 79 publications

References 59 publications

Mechanism of the AAA+ ATPases pontin and reptin in the biogenesis of H/ACA RNPs

Mechanism of the AAA+ ATPases pontin and reptin in the biogenesis of H/ACA RNPs

Characterization of hampin/MSL1 as a node in the nuclear interactome

Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex

Contact Info

Product

Resources

About