URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Regulation of (25)

ReferenceOther Genes Addressed
Kaplan CD, et al.  (2012) Dissection of Pol II Trigger Loop Function and Pol II Activity-Dependent Control of Start Site Selection In Vivo. PLoS Genet 8(4):e1002627
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Kryndushkin DS, et al.  (2011) Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 188(2):339-48
Higurashi T, et al.  (2008) Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci U S A 105(43):16596-601
Kryndushkin DS, et al.  (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J 27(20):2725-35
Kurahashi H, et al.  (2008) A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates. Mol Cell Biol 28(10):3313-23
Reineke LC, et al.  (2008) A Small Stem Loop Element Directs Internal Initiation of the URE2 Internal Ribosome Entry Site in Saccharomyces cerevisiae. J Biol Chem 283(27):19011-25
Savistchenko J, et al.  (2008) Molecular chaperones and the assembly of the prion ure2p in vitro. J Biol Chem 283(23):15732-9
Sharma D and Masison DC  (2008) Functionally redundant isoforms of a yeast hsp70 chaperone subfamily have different antiprion effects. Genetics 179(3):1301-11
Kryndushkin D and Wickner RB  (2007) Nucleotide Exchange Factors for Hsp70s Are Required for [URE3] Prion Propagation in Saccharomyces cerevisiae. Mol Biol Cell 18(6):2149-54
Komar AA, et al.  (2005) Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae eukaryotic initiation factor 2A. J Biol Chem 280(16):15601-11
Basu U, et al.  (2004) Reverse genetic analysis of the glutathione metabolic pathway suggests a novel role of PHGPX and URE2 genes in aluminum resistance in Saccharomyces cerevisiae. Mol Genet Genomics 271(5):627-37
Roberts BT, et al.  (2004) [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21(2):107-17
Komar AA, et al.  (2003) Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells. EMBO J 22(5):1199-209
Baxa U, et al.  (2002) Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein. Proc Natl Acad Sci U S A 99(8):5253-60
Cooper T  (2002) Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to the GATA factors: connecting the dots. FEMS Microbiol Rev 26(3):223-38
Fernandez-Bellot E, et al.  (2002) The [URE3] phenotype: evidence for a soluble prion in yeast. EMBO Rep 3(1):76-81
Jung G, et al.  (2002) Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc Natl Acad Sci U S A 99(15):9936-41
Sekito T, et al.  (2002) RTG-dependent mitochondria-to-nucleus signaling is regulated by MKS1 and is linked to formation of yeast prion [URE3]. Mol Biol Cell 13(3):795-804
Wickner RB, et al.  (2002) Prions of yeast as epigenetic phenomena: high protein "copy number" inducing protein "silencing". Adv Genet 46():485-525
van der Merwe GK, et al.  (2001) Ammonia regulates VID30 expression and Vid30p function shifts nitrogen metabolism toward glutamate formation especially when Saccharomyces cerevisiae is grown in low concentrations of ammonia. J Biol Chem 276(31):28659-66
Shamji AF, et al.  (2000) Partitioning the transcriptional program induced by rapamycin among the effectors of the Tor proteins. Curr Biol 10(24):1574-81
Beck T and Hall MN  (1999) The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors. Nature 402(6762):689-92
Cardenas ME, et al.  (1999) The TOR signaling cascade regulates gene expression in response to nutrients. Genes Dev 13(24):3271-9
Hardwick JS, et al.  (1999) Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteins. Proc Natl Acad Sci U S A 96(26):14866-70