RPS2/YGL123W Literature Guide Help

Other names published for RPS2: RPS4, SUP38, SUP44, SUP138, S2, S4, S5, Ys5, rp12, ribosomal 40S subunit protein S2, YGL123W

RPS2 - Strains/Constructs (25)

ReferenceOther Genes Addressed
Alhebshi A, et al.  (2012) The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species. Mol Biol Cell 23(18):3582-90
Fernandez-Pevida A, et al.  (2012) Yeast ribosomal protein L40 assembles late into precursor 60 S ribosomes and is required for their cytoplasmic maturation. J Biol Chem 287(45):38390-407
Steffen KK, et al.  (2012) Ribosome deficiency protects against ER stress in Saccharomyces cerevisiae. Genetics 191(1):107-18
Fassio CA, et al.  (2010) Dominant mutations in the late 40S biogenesis factor Ltv1 affect cytoplasmic maturation of the small ribosomal subunit in Saccharomyces cerevisiae. Genetics 185(1):199-209
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Gaillard H and Aguilera A  (2008) A novel class of mRNA-containing cytoplasmic granules are produced in response to UV-irradiation. Mol Biol Cell 19(11):4980-92
Kraft C, et al.  (2008) Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol 10(5):602-10
Zhang Y, et al.  (2008) Dre2, a conserved eukaryotic fe/s cluster protein, functions in cytosolic fe/s protein biogenesis. Mol Cell Biol 28(18):5569-82
Ferreira-Cerca S, et al.  (2007) Analysis of the in vivo assembly pathway of eukaryotic 40S ribosomal proteins. Mol Cell 28(3):446-57
Rother S and Strasser K  (2007) The RNA polymerase II CTD kinase Ctk1 functions in translation elongation. Genes Dev 21(11):1409-21
Dez C, et al.  (2006) Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae. EMBO J 25(7):1534-46
Panse VG, et al.  (2006) Formation and nuclear export of preribosomes are functionally linked to the small-ubiquitin-related modifier pathway. Traffic 7(10):1311-21
Ferreira-Cerca S, et al.  (2005) Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function. Mol Cell 20(2):263-75
Bernstein KA, et al.  (2004) The small-subunit processome is a ribosome assembly intermediate. Eukaryot Cell 3(6):1619-26
Galani K, et al.  (2004) Rea1, a dynein-related nuclear AAA-ATPase, is involved in late rRNA processing and nuclear export of 60 S subunits. J Biol Chem 279(53):55411-8
Milkereit P, et al.  (2003) A Noc complex specifically involved in the formation and nuclear export of ribosomal 40 S subunits. J Biol Chem 278(6):4072-81
Grandi P, et al.  (2002) 90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit processing factors but predominantly lack 60S synthesis factors. Mol Cell 10(1):105-15
Stansfield I, et al.  (1998) Missense translation errors in Saccharomyces cerevisiae. J Mol Biol 282(1):13-24
Synetos D, et al.  (1996) Mutations in yeast ribosomal proteins S28 and S4 affect the accuracy of translation and alter the sensitivity of the ribosomes to paromomycin. Biochim Biophys Acta 1309(1-2):156-66
Alksne LE, et al.  (1993) An accuracy center in the ribosome conserved over 2 billion years. Proc Natl Acad Sci U S A 90(20):9538-41
Ono B, et al.  (1991) Interactions between chromosomal omnipotent suppressors and extrachromosomal effectors in Saccharomyces cerevisiae. Curr Genet 19(4):243-8
All-Robyn JA, et al.  (1990) Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein. Mol Cell Biol 10(12):6544-53
Wakem LP and Sherman F  (1990) Isolation and characterization of omnipotent suppressors in the yeast Saccharomyces cerevisiae. Genetics 124(3):515-22
Ono B, et al.  (1989) Two new loci that give rise to dominant omnipotent suppressors in Saccharomyces cerevisiae. Curr Genet 16(5-6):323-30
Eustice DC, et al.  (1986) Altered 40 S ribosomal subunits in omnipotent suppressors of yeast. J Mol Biol 188(2):207-14