STO1/YMR125W Literature Guide Help

Other names published for STO1: CBC1, GCR3, CBP80, SUT1, YMR125W

STO1 - Strains/Constructs (28)

ReferenceOther Genes Addressed
Fell GL, et al.  (2011) Identification of yeast genes involved in k homeostasis: loss of membrane traffic genes affects k uptake. G3 (Bethesda) 1(1):43-56
Jung PP, et al.  (2011) Ploidy influences cellular responses to gross chromosomal rearrangements in Saccharomyces cerevisiae. BMC Genomics 12(1):331
Lahudkar S, et al.  (2011) The mRNA cap-binding complex stimulates the formation of pre-initiation complex at the promoter via its interaction with Mot1p in vivo. Nucleic Acids Res 39(6):2188-209
Bragulat M, et al.  (2010) RPL30 regulation of splicing reveals distinct roles for Cbp80 in U1 and U2 snRNP cotranscriptional recruitment. RNA 16(10):2033-41
Hage R, et al.  (2009) A targeted bypass screen identifies Ynl187p, Prp42p, Snu71p, and Cbp80p for stable U1 snRNP/Pre-mRNA interaction. Mol Cell Biol 29(14):3941-52
Hossain MA, et al.  (2009) The cap binding complex influences H2B ubiquitination by facilitating splicing of the SUS1 pre-mRNA. RNA 15(8):1515-27
Khanna M, et al.  (2009) A systematic characterization of Cwc21, the yeast ortholog of the human spliceosomal protein SRm300. RNA 15(12):2174-85
Wu X and Jiang YW  (2008) Overproduction of non-translatable mRNA silences. The transcription of Ty1 retrotransposons in S. cerevisiae via functional inactivation of the nuclear cap-binding complex and subsequent hyperstimulation of the TORC1 pathway. Yeast 25(5):327-47
McBride AE, et al.  (2007) Protein arginine methylation in Candida albicans: role in nuclear transport. Eukaryot Cell 6(7):1119-29
Das B, et al.  (2006) Mutant LYS2 mRNAs retained and degraded in the nucleus of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 103(29):10871-6
Gatbonton T, et al.  (2006) Telomere length as a quantitative trait: genome-wide survey and genetic mapping of telomere length-control genes in yeast. PLoS Genet 2(3):e35
Kim M, et al.  (2006) Distinct pathways for snoRNA and mRNA termination. Mol Cell 24(5):723-34
Burckin T, et al.  (2005) Exploring functional relationships between components of the gene expression machinery. Nat Struct Mol Biol 12(2):175-82
Gao Q, et al.  (2005) Cap-binding protein 1-mediated and eukaryotic translation initiation factor 4E-mediated pioneer rounds of translation in yeast. Proc Natl Acad Sci U S A 102(12):4258-63
Gornemann J, et al.  (2005) Cotranscriptional spliceosome assembly occurs in a stepwise fashion and requires the cap binding complex. Mol Cell 19(1):53-63
Kuai L, et al.  (2005) A nuclear degradation pathway controls the abundance of normal mRNAs in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 102(39):13962-7
McBride AE, et al.  (2005) Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions. J Biol Chem 280(35):30888-98
Askree SH, et al.  (2004) A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc Natl Acad Sci U S A 101(23):8658-63
Windgassen M, et al.  (2004) Yeast shuttling SR proteins Npl3p, Gbp2p, and Hrb1p are part of the translating mRNPs, and Npl3p can function as a translational repressor. Mol Cell Biol 24(23):10479-91
Baron-Benhamou J, et al.  (2003) The interaction of the cap-binding complex (CBC) with eIF4G is dispensable for translation in yeast. RNA 9(6):654-62
Das B, et al.  (2003) Degradation of normal mRNA in the nucleus of Saccharomyces cerevisiae. Mol Cell Biol 23(16):5502-15
Kushner DB, et al.  (2003) Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus. Proc Natl Acad Sci U S A 100(26):15764-9
Das B, et al.  (2000) The role of nuclear cap binding protein Cbc1p of yeast in mRNA termination and degradation. Mol Cell Biol 20(8):2827-38
Fortes P, et al.  (2000) The yeast nuclear cap binding complex can interact with translation factor eIF4G and mediate translation initiation. Mol Cell 6(1):191-6
Shen EC, et al.  (2000) 7The yeast mRNA-binding protein Npl3p interacts with the cap-binding complex. J Biol Chem 275(31):23718-24
Fortes P, et al.  (1999) Genetic and physical interactions involving the yeast nuclear cap-binding complex. Mol Cell Biol 19(10):6543-53
Uemura H, et al.  (1996) Mutations in GCR3, a gene involved in the expression of glycolytic genes in Saccharomyces cerevisiae, suppress the temperature-sensitive growth of hpr1 mutants. Genetics 142(4):1095-103
Uemura H and Jigami Y  (1992) GCR3 encodes an acidic protein that is required for expression of glycolytic genes in Saccharomyces cerevisiae. J Bacteriol 174(17):5526-32