Fcf1p and Fcf2p are novel nucleolar Saccharomyces cerevisiae proteins involved in pre-rRNA processing

Rempoła, Bożenna; Karkusiewicz, Iwona; Piekarska, Iga; Rytka, Joanna

doi:10.1016/j.bbrc.2006.05.140

Cited by 22 publications

(24 citation statements)

References 36 publications

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“…S3A for location of the probes). In line with previous reports, 39,40 we noted that yUtp24 dysfunction (irrespective of whether yUtp24 levels were low or the putative enzymatic activity of the protein was abolished) resulted in a significant decrease of mature 18S rRNA. This was accompanied by a marked reduction of 20S prerRNA (Fig.…”

supporting

confidence: 93%

“…It was previously suggested that a protein with a PIN nuclease domain, namely yUtp24 (also called Fcf1), might be involved in the endoribonucleolytic cleavage of yeast pre-rRNA at sites A 0 in the 5 0 -ETS and A 1 , thus forming a mature 18S 5 0 -end, and at site A 2 (which was later shown to be processed by a controversial endoribonucleolytic activity of Rcl1 protein, similar to RNA 3 0 cyclases). [39][40][41][42] Nevertheless, yUtp24 has not been shown to have enzymatic activity in vitro, and in vivo analyses, such as primer extensionbased mapping of the processing sites affected by yUtp24 mutation, have not been performed to date. In this study, we analyzed the role of yUtp24 orthologhUTP24 -in pre-rRNA processing in human cells.…”

mentioning

confidence: 99%

“…39,40 Northern blot analyses and pulse-chase RNA labeling experiments revealed that its presence in the cell seemed to be indispensable for cleavage at site A 0 in the 5 0 -ETS, while its putative ribonucleolytic activity appeared to be necessary for processing at sites A 1 and A 2 (see Fig. 3A for positioning of the processing sites in yeast pre-rRNA).…”

mentioning

confidence: 99%

“…48 A direct identification of Faf1-interacting proteins by tandem affinity purification followed by mass spectrometry revealed that yUtp24 is among numerous yeast SSU processome constituents that co-purify with the bait protein. 40 To verify whether yUtp24 is a genuine component of the SSU processome in S. cerevisiae, we performed reciprocal purifications of TAP-tagged yUtp24 WT and mut (to ensure that the catalytic mutation does not affect incorporation of the protein of interest into the assembly) from yeast strains producing fusion proteins under the control of the endogenous promoter, and then analyzed proteins present in the eluates using high resolution mass spectrometry and MaxQuant software for quantification. The results were compared to those obtained from the non-transformed parental yeast strain, which was subjected to the same purification procedure in parallel.…”

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confidence: 99%

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hUTP24 is essential for processing of the human rRNA precursor at site A₁, but not at site A₀

et al. 2015

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Production of ribosomes relies on more than 200 accessory factors to ensure the proper sequence of steps and faultless assembly of ribonucleoprotein machinery. Among trans-acting factors are numerous enzymes, including ribonucleases responsible for processing the large rRNA precursor synthesized by RNA polymerase I that encompasses sequences corresponding to mature 18S, 5.8S, and 25/28S rRNA. In humans, the identity of most enzymes responsible for individual processing steps, including endoribonucleases that cleave pre-rRNA at specific sites within regions flanking and separating mature rRNA, remains largely unknown. Here, we investigated the role of hUTP24 in rRNA maturation in human cells. hUTP24 is a human homolog of the Saccharomyces cerevisiae putative PIN domaincontaining endoribonuclease Utp24 (yUtp24), which was suggested to participate in the U3 snoRNA-dependent processing of yeast pre-rRNA at sites A 0 , A 1 , and A 2 . We demonstrate that hUTP24 interacts to some extent with proteins homologous to the components of the yeast small subunit (SSU) processome. Moreover, mutation in the putative catalytic site of hUTP24 results in slowed growth of cells and reduced metabolic activity. These effects are associated with a defect in biogenesis of the 40S ribosomal subunit, which results from decreased amounts of 18S rRNA as a consequence of inaccurate pre-rRNA processing at the 5 0 -end of the 18S rRNA segment (site A 1 ). Interestingly, and in contrast to yeast, site A 0 located upstream of A 1 is efficiently processed upon UTP24 dysfunction. Finally, hUTP24 inactivation leads to aberrant processing of 18S rRNA 2 nucleotides downstream of the normal A 1 cleavage site.

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hUTP24 is essential for processing of the human rRNA precursor at site A₁, but not at site A₀

et al. 2015

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“…In this study, we find that Rrp14p interacts with Utp11p and Faf1p. It was demonstrated that Utp11p is a component of the SSU processome and Faf1p associates with a large number of components of SSU (Dragon et al 2002;Rempola et al 2006). Interestingly, Faf1p was categorized as a middle-strength transcription activator in systematic analysis using the yeast onehybrid system (Titz et al 2006).…”

Section: Rrp14p Has a Role In Ribosome Biogenesismentioning

confidence: 99%

Yeast Rrp14p is a nucleolar protein involved in both ribosome biogenesis and cell polarity

Yamada

Horigome

Okada

et al. 2007

RNA

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We previously cloned RRP14/YKL082c, whose product exhibits two-hybrid interaction with Ebp2p, a regulatory factor of assembly of 60S ribosomal subunits. Depletion of Rrp14p results in shortage of 60S ribosomal subunits and retardation of processing from 27S pre-rRNA to 25S rRNA. Furthermore, 35S pre-rRNA synthesis appears to decline in Rrp14p-depleted cells. Rrp14p interacts with regulatory factors of 60S subunit assembly and also with Utp11p and Faf1p, which are regulatory factors required for assembly of 40S ribosomal subunits. We propose that Rrp14p is involved in ribosome synthesis from the beginning of 35S pre-rRNA synthesis to assembly of the 60S ribosomal subunit. Disruption of RRP14 causes an extremely slow growth rate of the cell, a severe defect in ribosome synthesis, and a depolarized localization of cortical actin patches throughout the cell cycle. These results suggest that Rrp14p has dual functions in ribosome synthesis and polarized cell growth.

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Comparison of preribosomal RNA processing pathways in yeast, plant and human cells – focus on coordinated action of endo‐ and exoribonucleases

2017

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Edited by Michael IbbaProper regulation of ribosome biosynthesis is mandatory for cellular adaptation, growth and proliferation. Ribosome biogenesis is the most energetically demanding cellular process, which requires tight control. Abnormalities in ribosome production have severe consequences, including developmental defects in plants and genetic diseases (ribosomopathies) in humans. One of the processes occurring during eukaryotic ribosome biogenesis is processing of the ribosomal RNA precursor molecule (pre-rRNA), synthesized by RNA polymerase I, into mature rRNAs. It must not only be accurate but must also be precisely coordinated with other phenomena leading to the synthesis of functional ribosomes: RNA modification, RNA folding, assembly with ribosomal proteins and nucleocytoplasmic RNP export. A multitude of ribosome biogenesis factors ensure that these events take place in a correct temporal order. Among them are endo-and exoribonucleases involved in pre-rRNA processing. Here, we thoroughly present a wide spectrum of ribonucleases participating in rRNA maturation, focusing on their biochemical properties, regulatory mechanisms and substrate specificity. We also discuss cooperation between various ribonucleolytic activities in particular stages of pre-rRNA processing, delineating major similarities and differences between three representative groups of eukaryotes: yeast, plants and humans.Keywords: endoribonuclease; exoribonuclease; pre-rRNA processing; ribosome biogenesis; RNA quality control; RNA trimming Ribosome biosynthesis is a multistep process that includes several tightly controlled events -ribosomal DNA (rDNA) transcription, processing of rRNA precursors into mature molecules, accompanied by binding of ribosome biogenesis factors (RBFs) and ribosomal proteins (RPs), and the final assembly of all Abbreviations CD, catalytic domain; dsRBD, double-stranded RNA-binding domain; ETS, external transcribed spacer; ITS, internal transcribed spacer; LSU, large ribosome subunit (60S); miRNA, microRNA; mRNA, messenger RNA; MRP RNA, noncoding RNA component of the RNase MRP; mTOR, mammalian target of rapamycin; nt(s), nucleotide(s); PIN domain, PilT N-terminal domain; Pol I/II/III, RNA polymerase I/II/III; prerRNA, ribosomal RNA precursor; RBF, ribosome biogenesis factor; RMRP, RNase MRP (mitochondrial RNA processing ribonuclease); RNase, ribonuclease; RNB domain, RNase II domain; RNP, ribonucleoprotein; RP, ribosomal protein; rRNA, ribosomal RNA; siRNA, short interfering RNA; snoRNA, small nucleolar RNA; snoRNP, small nucleolar ribonucleoprotein; snRNA, small nuclear RNA; SSU, small ribosome subunit (40S); TRAMP4 or TRAMP5, Trf4/Air/Mtr4 or Trf5/Air/Mtr4 polyadenylation complex; tRNA, transfer RNA.

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Fcf1p and Fcf2p are novel nucleolar Saccharomyces cerevisiae proteins involved in pre-rRNA processing

Cited by 22 publications

References 36 publications

hUTP24 is essential for processing of the human rRNA precursor at site A₁, but not at site A₀

hUTP24 is essential for processing of the human rRNA precursor at site A₁, but not at site A₀

Yeast Rrp14p is a nucleolar protein involved in both ribosome biogenesis and cell polarity

Comparison of preribosomal RNA processing pathways in yeast, plant and human cells – focus on coordinated action of endo‐ and exoribonucleases

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Fcf1p and Fcf2p are novel nucleolar Saccharomyces cerevisiae proteins involved in pre-rRNA processing

Cited by 22 publications

References 36 publications

hUTP24 is essential for processing of the human rRNA precursor at site A1, but not at site A0

hUTP24 is essential for processing of the human rRNA precursor at site A1, but not at site A0

Yeast Rrp14p is a nucleolar protein involved in both ribosome biogenesis and cell polarity

Comparison of preribosomal RNA processing pathways in yeast, plant and human cells – focus on coordinated action of endo‐ and exoribonucleases

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hUTP24 is essential for processing of the human rRNA precursor at site A₁, but not at site A₀

hUTP24 is essential for processing of the human rRNA precursor at site A₁, but not at site A₀