CBF5/YLR175W Literature Guide Help

Other names published for CBF5: pseudouridine synthase CBF5, YLR175W

CBF5 - Strains/Constructs (25)

ReferenceOther Genes Addressed
Jack K, et al.  (2011) rRNA Pseudouridylation Defects Affect Ribosomal Ligand Binding and Translational Fidelity from Yeast to Human Cells. Mol Cell 44(4):660-6
Jung PP, et al.  (2011) Ploidy influences cellular responses to gross chromosomal rearrangements in Saccharomyces cerevisiae. BMC Genomics 12(1):331
Lemay V, et al.  (2011) Identification of novel proteins associated with yeast snR30 small nucleolar RNA. Nucleic Acids Res 39(22):9659-70
Li S, et al.  (2011) Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita.LID - 10.1038/emboj.2011.427 [doi] EMBO J ()
Walbott H, et al.  (2011) The H/ACA RNP assembly factor SHQ1 functions as an RNA mimic. Genes Dev 25(22):2398-408
Godin KS, et al.  (2009) The box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme. J Mol Biol 390(2):231-44
Ungar L, et al.  (2009) A genome-wide screen for essential yeast genes that affect telomere length maintenance. Nucleic Acids Res 37(12):3840-9
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Decatur WA and Schnare MN  (2008) Different mechanisms for Pseudouridine formation in yeast 5S and 5.8S rRNAs. Mol Cell Biol 28(10):3089-100
Hoskins J and Butler JS  (2008) RNA-Based 5-Fluorouracil Toxicity Requires the Pseudouridylation Activity of Cbf5p. Genetics 179(1):323-30
Normand C, et al.  (2006) Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA. RNA 12(10):1868-82
Ballarino M, et al.  (2005) The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae. Mol Cell Biol 25(13):5396-403
Ma X, et al.  (2005) Pseudouridylation of yeast U2 snRNA is catalyzed by either an RNA-guided or RNA-independent mechanism. EMBO J 24(13):2403-13
Yang PK, et al.  (2005) Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly. Mol Cell Biol 25(8):3295-304
Henras AK, et al.  (2004) Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA snoRNAs. RNA 10(11):1704-12
Kendall A, et al.  (2000) A CBF5 mutation that disrupts nucleolar localization of early tRNA biosynthesis in yeast also suppresses tRNA gene-mediated transcriptional silencing. Proc Natl Acad Sci U S A 97(24):13108-13
Massenet S, et al.  (1999) Pseudouridine mapping in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (snRNAs) reveals that pseudouridine synthase pus1p exhibits a dual substrate specificity for U2 snRNA and tRNA. Mol Cell Biol 19(3):2142-54
Zebarjadian Y, et al.  (1999) Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA. Mol Cell Biol 19(11):7461-72
Lafontaine DLJ, et al.  (1998) The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase. Genes Dev 12(4):527-37
Phillips B, et al.  (1998) The Nop60B gene of Drosophila encodes an essential nucleolar protein that functions in yeast. Mol Gen Genet 260(1):20-9
Winkler AA, et al.  (1998) The lysine-rich C-terminal repeats of the centromere-binding factor 5 (Cbf5) of Kluyveromyces lactis are not essential for function. Yeast 14(1):37-48
Cadwell C, et al.  (1997) The yeast nucleolar protein Cbf5p is involved in rRNA biosynthesis and interacts genetically with the RNA polymerase I transcription factor RRN3. Mol Cell Biol 17(10):6175-83
Ganot P, et al.  (1997) Site-specific pseudouridine formation in preribosomal RNA is guided by small nucleolar RNAs. Cell 89(5):799-809
Ni J, et al.  (1997) Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA. Cell 89(4):565-73
Jiang W, et al.  (1993) An essential yeast protein, CBF5p, binds in vitro to centromeres and microtubules. Mol Cell Biol 13(8):4884-93