RPS3/YNL178W Literature Guide Help

Other names published for RPS3: SUF14, S3, YS3, rp13, ribosomal 40S subunit protein S3, YNL178W

RPS3 - Protein-protein Interactions (24)

ReferenceOther Genes Addressed
Karaskova M, et al.  (2012) Functional characterization of the role of the N-terminal domain of the c/Nip1 subunit of eukaryotic initiation factor 3 (eIF3) in AUG recognition. J Biol Chem 287(34):28420-34
Koch B, et al.  (2012) Yar1 protects the ribosomal protein Rps3 from aggregation. J Biol Chem 287(26):21806-15
Tudisca V, et al.  (2012) PKA isoforms coordinate mRNA fate during nutrient starvation. J Cell Sci 125(Pt 21):5221-32
Campbell MG and Karbstein K  (2011) Protein-protein interactions within late pre-40S ribosomes. PLoS One 6(1):e16194
Drummond SP, et al.  (2011) Diauxic shift-dependent relocalization of decapping activators Dhh1 and Pat1 to polysomal complexes. Nucleic Acids Res 39(17):7764-74
Strunk BS, et al.  (2011) Ribosome assembly factors prevent premature translation initiation by 40S assembly intermediates. Science 333(6048):1449-53
Chiu WL, et al.  (2010) The C-Terminal Region of Eukaryotic Translation Initiation Factor 3a (eIF3a) Promotes mRNA Recruitment, Scanning, and, Together with eIF3j and the eIF3b RNA Recognition Motif, Selection of AUG Start Codons. Mol Cell Biol 30(18):4415-34
Cuchalova L, et al.  (2010) The RNA Recognition Motif of Eukaryotic Translation Initiation Factor 3g (eIF3g) Is Required for Resumption of Scanning of Posttermination Ribosomes for Reinitiation on GCN4 and Together with eIF3i Stimulates Linear Scanning. Mol Cell Biol 30(19):4671-86
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
Granneman S, et al.  (2010) Cracking pre-40S ribosomal subunit structure by systematic analyses of RNA-protein cross-linking. EMBO J 29(12):2026-36
Kuroha K, et al.  (2010) Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest. EMBO Rep 11(12):956-61
Nanda JS, et al.  (2009) eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J Mol Biol 394(2):268-85
Passmore LA, et al.  (2007) The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol Cell 26(1):41-50
Swatkoski S, et al.  (2007) Integration of Residue-Specific Acid Cleavage into Proteomic Workflows. J Proteome Res 6(11):4525-4527
Schafer T, et al.  (2006) Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit. Nature 441(7093):651-5
Algire MA, et al.  (2005) Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol Cell 20(2):251-62
Fekete CA, et al.  (2005) The eIF1A C-terminal domain promotes initiation complex assembly, scanning and AUG selection in vivo. EMBO J 24(20):3588-601
Hoang T, et al.  (2005) Esf2p, a U3-associated factor required for small-subunit processome assembly and compaction. Mol Cell Biol 25(13):5523-34
Loar JW, et al.  (2004) Genetic and biochemical interactions among Yar1, Ltv1 and Rps3 define novel links between environmental stress and ribosome biogenesis in Saccharomyces cerevisiae. Genetics 168(4):1877-89
Spahn CM, et al.  (2004) Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J 23(5):1008-19
George R, et al.  (2002) The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo. FEBS Lett 516(1-3):213-6
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
Menetret JF, et al.  (2000) The structure of ribosome-channel complexes engaged in protein translocation. Mol Cell 6(5):1219-32
Yeh YC, et al.  (1986) Protein topography of the 40 S ribosomal subunit from Saccharomyces cerevisiae as shown by chemical cross-linking. J Biol Chem 261(30):14148-53