Functional and physical interactions of Faf1p, a Saccharomyces cerevisiae nucleolar protein

Karkusiewicz, Iwona; Rempoła, Bożenna; Gromadka, Robert; Grynberg, Marcin; Rytka, Joanna

doi:10.1016/j.bbrc.2004.05.012

Cited by 10 publications

(12 citation statements)

References 40 publications

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“…ComplexKrr1 and Faf1 were previously reported to interact with each other in a two-hybrid assay (37). We confirmed their physical interaction with a GST pulldown assay using recombinant proteins.…”

Section: Structure Determination Of the Krr1 And Faf1supporting

confidence: 81%

“…Besides putative RNA binding activity, Krr1 also binds proteins. It binds Faf1 in a yeast two-hybrid assay (37) and interacts genetically and physically with Kri1, which is another factor essential for 40 S formation (34). Krr1 is universally conserved in eukaryotes, and its orthologs in Drosophila, Schizosaccharomyces pombe, and humans have been shown to be involved in ribosome biogenesis (40 -42).…”

mentioning

confidence: 99%

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Interaction between Ribosome Assembly Factors Krr1 and Faf1 Is Essential for Formation of Small Ribosomal Subunit in Yeast

Zheng

Lan

Liu

et al. 2014

Journal of Biological Chemistry

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Background:The 90 S precursor of small ribosomal subunits is an enormous and poorly understood structure. Results: A subcomplex structure of 90 S proteins Krr1 and Faf1 was determined. Conclusion: The KH domains of Krr1 are versatile in protein interaction, and the Krr1-Faf1 interaction is essential for forming functional 90 S pre-ribosomes. Significance: The study provides structural and functional insight of a protein-protein interaction within 90 S pre-ribosomes.

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Section: Structure Determination Of the Krr1 And Faf1supporting

confidence: 81%

mentioning

confidence: 99%

Interaction between Ribosome Assembly Factors Krr1 and Faf1 Is Essential for Formation of Small Ribosomal Subunit in Yeast

Zheng

Lan

Liu

et al. 2014

Journal of Biological Chemistry

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“…The processing activity of the 18S-1770 particle could be accounted for by its nearly complete set of AFs. However, the Faf1 protein essential for 5 ′ ETS processing was not found (Karkusiewicz et al 2004;Shirai et al 2004;Zheng et al 2014). The association of Faf1 is quite variable, and we cannot exclude that a small amount of Faf1 still associated with 18S-1770 but escaped detection.…”

Section: Processing Of the 5 ′ Etsmentioning

confidence: 89%

“…The ITS1-3 RNA that contains the complete 18S region recruited the last protein, Faf1, in our map (Karkusiewicz et al 2004;Shirai et al 2004;Zheng et al 2014). The amount of Faf1 was quite variable in different purifications and particles.…”

Section: Assembly Of Thementioning

confidence: 95%

Stepwise and dynamic assembly of the earliest precursors of small ribosomal subunits in yeast

et al. 2016

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The eukaryotic ribosomal RNA (rRNA) is associated cotranscriptionally with numerous factors into an enormous 90S preribosomal particle that conducts early processing of small ribosomal subunits. The assembly pathway and structure of the 90S particle is poorly understood. Here, we affinity-purified and analyzed the constituents of yeast 90S particles that were assembled on a series of plasmid-encoded 3 ′ -truncated pre-18S RNAs. We determined the assembly point of 65 proteins and the U3, U14, and snR30 small nucleolar RNAs (snoRNAs), revealing a stepwise and dynamic assembly map. The 5 ′ external transcribed spacer (ETS) alone can nucleate a large complex. When the 18S rRNA is nearly complete, the 90S structure undergoes a dramatic reorganization, releasing U14, snR30, and 14 protein factors that bind earlier. We also identified a reference state of 90S that is fully assembled yet has not undergone 5 ′ ETS processing. The assembly map present here provides a new framework to understand small subunit biogenesis.

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“…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.…”

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confidence: 99%

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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Functional and physical interactions of Faf1p, a Saccharomyces cerevisiae nucleolar protein

Cited by 10 publications

References 40 publications

Interaction between Ribosome Assembly Factors Krr1 and Faf1 Is Essential for Formation of Small Ribosomal Subunit in Yeast

Interaction between Ribosome Assembly Factors Krr1 and Faf1 Is Essential for Formation of Small Ribosomal Subunit in Yeast

Stepwise and dynamic assembly of the earliest precursors of small ribosomal subunits in yeast

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

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Functional and physical interactions of Faf1p, a Saccharomyces cerevisiae nucleolar protein

Cited by 10 publications

References 40 publications

Interaction between Ribosome Assembly Factors Krr1 and Faf1 Is Essential for Formation of Small Ribosomal Subunit in Yeast

Interaction between Ribosome Assembly Factors Krr1 and Faf1 Is Essential for Formation of Small Ribosomal Subunit in Yeast

Stepwise and dynamic assembly of the earliest precursors of small ribosomal subunits in yeast

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

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