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Gene Review

CBF5  -  pseudouridine synthase CBF5

Saccharomyces cerevisiae S288c

Synonyms: Centromere-binding factor 5, Centromere/microtubule-binding protein CBF5, H/ACA ribonucleoprotein complex subunit 4, H/ACA snoRNP protein CBF5, L9470.11, ...
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Disease relevance of CBF5


High impact information on CBF5

  • The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase [2].
  • Using the snR81-deletion strain, Nhp2p- or Cbf5p-conditional depletion strain, and a cbf5 mutation strain, we further demonstrated that the pseudouridylase activity is dependent on snR81 snoRNP in vivo [3].
  • A CBF5 mutation that disrupts nucleolar localization of early tRNA biosynthesis in yeast also suppresses tRNA gene-mediated transcriptional silencing [4].
  • Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly [5].
  • Naf1p and Cbf5p cross-link predominantly with the 3' end of these genes, in a pattern similar to that observed for transcription elongation factor Spt16p [5].

Biological context of CBF5


Anatomical context of CBF5

  • Our results provide additional evidence that Cbf5p is the Psi synthase component of box H/ACA snoRNPs and suggest that the pseudouridylation of rRNA, although not absolutely required for cell survival, is essential for the formation of fully functional ribosomes [1].

Associations of CBF5 with chemical compounds


Physical interactions of CBF5


Regulatory relationships of CBF5

  • In yeast, Naf1p interacts with H/ACA snoRNP proteins and may promote assembly of Cbf5p (the yeast ortholog of dyskerin) with nascent pre-snoRNAs [12].

Other interactions of CBF5

  • Indeed, depletion of Naf1p leads to a specific and dramatic decrease in the steady-state accumulation of all box H/ACA snoRNAs tested and of Cbf5p, Gar1p, and Nop10p [13].
  • We also provide further in vivo evidence that Mck1p, a protein kinase, is specifically associated with the centromere proteins Cbf2p and Cbf5p, which were previously shown to interact in vitro [14].
  • Unexpectedly, we identified multiple SL mutations that were complemented by Cbf5p and Nop58p [15].
  • Putative homologs of the kinetochore protein SKP1 (suppressor of kinetochore protein 1p of yeast) were found in both species and of CBF5p (centromere binding factor 5 of yeast) in barley [16].
  • Chromatin immunoprecipitation experiments show that Naf1p and the pseudouridylsynthetase Cbf5p cross-link specifically with the chromatin of H/ACA small nucleolar RNA (snoRNA) genes [5].

Analytical, diagnostic and therapeutic context of CBF5

  • Immunoprecipitation studies using either anti-Cbf5p antibodies or a hemagglutinin-tagged Nhp2p demonstrated that both proteins are associated with all H/ACA-motif snoRNPs [17].
  • Sequence analysis of the individual polypeptides demonstrated that the three proteins Gar1p, Nhp2p, and Cbf5p are common to both the snR30 and snR42 complexes [17].
  • A reverse transcription-polymerase chain reaction (RT-PCR) approach was used to clone a cDNA encoding the EUGLENA: gracilis homolog of yeast Cbf5p, a protein component of the box H/ACA class of snoRNPs that mediate pseudouridine formation in eukaryotic rRNA [18].


  1. Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA. Zebarjadian, Y., King, T., Fournier, M.J., Clarke, L., Carbon, J. Mol. Cell. Biol. (1999) [Pubmed]
  2. The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase. Lafontaine, D.L., Bousquet-Antonelli, C., Henry, Y., Caizergues-Ferrer, M., Tollervey, D. Genes Dev. (1998) [Pubmed]
  3. Pseudouridylation of yeast U2 snRNA is catalyzed by either an RNA-guided or RNA-independent mechanism. Ma, X., Yang, C., Alexandrov, A., Grayhack, E.J., Behm-Ansmant, I., Yu, Y.T. EMBO J. (2005) [Pubmed]
  4. A CBF5 mutation that disrupts nucleolar localization of early tRNA biosynthesis in yeast also suppresses tRNA gene-mediated transcriptional silencing. Kendall, A., Hull, M.W., Bertrand, E., Good, P.D., Singer, R.H., Engelke, D.R. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly. Yang, P.K., Hoareau, C., Froment, C., Monsarrat, B., Henry, Y., Chanfreau, G. Mol. Cell. Biol. (2005) [Pubmed]
  6. An essential yeast protein, CBF5p, binds in vitro to centromeres and microtubules. Jiang, W., Middleton, K., Yoon, H.J., Fouquet, C., Carbon, J. Mol. Cell. Biol. (1993) [Pubmed]
  7. The lysine-rich C-terminal repeats of the centromere-binding factor 5 (Cbf5) of Kluyveromyces lactis are not essential for function. Winkler, A.A., Bobok, A., Zonneveld, B.J., Steensma, H.Y., Hooykaas, P.J. Yeast (1998) [Pubmed]
  8. The yeast nucleolar protein Cbf5p is involved in rRNA biosynthesis and interacts genetically with the RNA polymerase I transcription factor RRN3. Cadwell, C., Yoon, H.J., Zebarjadian, Y., Carbon, J. Mol. Cell. Biol. (1997) [Pubmed]
  9. Cloning and characterization of Arabidopsis thaliana AtNAP57--a homologue of yeast pseudouridine synthase Cbf5p. Maceluch, J., Kmieciak, M., Szweykowska-Kulińska, Z., Jarmołowski, A. Acta Biochim. Pol. (2001) [Pubmed]
  10. Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein. Sydorskyy, Y., Dilworth, D.J., Halloran, B., Yi, E.C., Makhnevych, T., Wozniak, R.W., Aitchison, J.D. Biochem. J. (2005) [Pubmed]
  11. Naf1 p is a box H/ACA snoRNP assembly factor. Fatica, A., Dlakić, M., Tollervey, D. RNA (2002) [Pubmed]
  12. hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs, and telomerase. Hoareau-Aveilla, C., Bonoli, M., Caizergues-Ferrer, M., Henry, Y. RNA (2006) [Pubmed]
  13. Naf1p, an essential nucleoplasmic factor specifically required for accumulation of box H/ACA small nucleolar RNPs. Dez, C., Noaillac-Depeyre, J., Caizergues-Ferrer, M., Henry, Y. Mol. Cell. Biol. (2002) [Pubmed]
  14. Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae. Jiang, W., Koltin, Y. Mol. Gen. Genet. (1996) [Pubmed]
  15. Genetic and physical interactions involving the yeast nuclear cap-binding complex. Fortes, P., Kufel, J., Fornerod, M., Polycarpou-Schwarz, M., Lafontaine, D., Tollervey, D., Mattaj, I.W. Mol. Cell. Biol. (1999) [Pubmed]
  16. Evolutionary conservation of kinetochore protein sequences in plants. ten Hoopen, R., Manteuffel, R., Dolezel, J., Malysheva, L., Schubert, I. Chromosoma (2000) [Pubmed]
  17. Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure. Watkins, N.J., Gottschalk, A., Neubauer, G., Kastner, B., Fabrizio, P., Mann, M., Lührmann, R. RNA (1998) [Pubmed]
  18. Evolutionary appearance of genes encoding proteins associated with box H/ACA snoRNAs: cbf5p in Euglena gracilis, an early diverging eukaryote, and candidate Gar1p and Nop10p homologs in archaebacteria. Watanabe, Y., Gray, M.W. Nucleic Acids Res. (2000) [Pubmed]
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