Molecular cloning and characterization of Nop25, a novel nucleolar RNA binding protein, highly conserved in vertebrate species

Suzuki, Shunji; Kanno, Motoko; Fujiwara, Takashi; Sugiyama, H.; Yokoyama, Akiko; Takahashi, Hiroyuki; Tanaka, Junya

doi:10.1016/j.yexcr.2005.12.017

Cited by 9 publications

(9 citation statements)

References 33 publications

(45 reference statements)

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“…It has been reported that Rrp15p, a homologous protein of the Rrp15 protein, is involved in the synthesis of large subunit rRNA . To determine if the Rrp15 protein has a similar function, GFP‐labeled NIH3T3 cells overexpressing Rrp15 were fixed with or without RNase digestion.…”

Section: Resultsmentioning

confidence: 99%

“…This allowed RNase to digest the RNA, including pre‐RNA, mature RNA, rRNA, and microRNA, into smaller fragments. Proteins participating in RNA processing are removed following RNase digestion in the nucleus . The process of ribosome assembly is evolutionally conserved .…”

Section: Discussionmentioning

confidence: 99%

“…Proteins participating in RNA processing are removed following RNase digestion in the nucleus . The process of ribosome assembly is evolutionally conserved . RRP15p is a component of the pre‐60S ribosome in the nucleus and depletion of the RRP15p gene inhibits the accumulation of several pre‐rRNA of the 60S ribosome .…”

Section: Discussionmentioning

confidence: 99%

“…The process of ribosome assembly is evolutionally conserved . RRP15p is a component of the pre‐60S ribosome in the nucleus and depletion of the RRP15p gene inhibits the accumulation of several pre‐rRNA of the 60S ribosome . The function of the Rrp15 protein in pre‐rRNA maturation should be investigated in future studies.…”

Section: Discussionmentioning

confidence: 99%

“…This is a key preparatory step in the assembly of large and small subunits of ribosomes . Several reports have indicated that ribosomal processing proteins are highly evolutionarily conserved in eukaryotes . In higher level organisms, there are many proteins that demonstrate homology to the RNA processing factors of yeast, for example, Nop25 , Nop52, and Bop1.…”

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confidence: 99%

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Rrp15 affects cell cycle, proliferation, and apoptosis in NIH3T3 cells

Ren

Chen

et al. 2016

FEBS Open Bio

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Riken 2810430M08 (hereinafter referred to as Rrp15) is a newly identified and reported gene from the mouse genome. In our previous work, we found that the gene had a relationship with the proliferation and activation of T cells. Rrp15 protein is highly homologous with RRP15 (budding yeast), which has an important role in ribosomal RNA processing. We explored the potential function of Rrp15 in apoptosis, cell proliferation, and its involvement with RNA in the nucleus. We constructed a knockdown of the Rrp15 gene in NIH3T3 cells and then performed real‐time PCR, western blotting, flow cytometry, and immunofluorescence to determine the function of the Rrp15 gene. Knockdown of the Rrp15 gene suppresses proliferation and induces apoptosis. We also found that the Rrp15 protein was normally distributed in the nucleus and bound to RNA or pre‐RNA in the nucleus. Additionally, Rrp15 altered the activity of the 20S proteasome. Rrp15 promotes proliferation and inhibits apoptosis in NIH3T3 cells and may have a relationship with RNA in the nucleus.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Rrp15 affects cell cycle, proliferation, and apoptosis in NIH3T3 cells

Ren

Chen

et al. 2016

FEBS Open Bio

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Characterizing the novel protein p33MONOX

2010

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The novel protein p33MONOX (p33Monooxygenase) was over-expressed in neuroblastoma cells demonstrating its inhibitory effect on the phosphorylation of the App (amyloid precursor protein) and Bcl2 (B-cell lymphoma 2) proteins but mediating higher activation of Mapk1/3 (mitogen-activated protein kinase 1/3). We employed a variety of cell biology techniques to show the localization of p33MONOX to the cytoplasm of pyramidal neurons in the mouse brain hippocampus. We also carried out a yeast-two-hybrid screening plus co-immunoprecipitation and bio-informatics to determine COBRA1 (cofactor of BRCA1 (breast cancer type 1)), NOL12 (nucleolar protein 12), and PRNP (prion protein) as p33MONOX-interacting proteins. Bio-computational analyses revealed a flavine-containing monooxygenase (FMO)-1 motif, thus linking p33MONOX to a group of previously characterized proteins, the MICALs (molecule interacting with CasL). Concluding, p33MONOX might regulate pre- and post-transcriptional control of dynamic processes related to growth cone guidance.

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