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Gene Review

PRT1  -  Prt1p

Saccharomyces cerevisiae S288c

Synonyms: CDC63, Cell cycle regulation and translation initiation protein, DNA26, Eukaryotic translation initiation factor 3 90 kDa subunit, Eukaryotic translation initiation factor 3 subunit B, ...
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High impact information on PRT1

  • By characterizing the mutant subcomplexes, we confirmed all key predictions of our model and uncovered new interactions of NIP1 with PRT1 and of TIF32 with eIF1 [1].
  • Thus, several key functions of eIF3 can be carried out by the PRT1-TIF32-NIP1 subcomplex [2].
  • Our results provide support for both physical and functional interactions between three subunits, TIF34, PRT1 and p33, in the eIF3 complex [3].
  • Yeast prt1 mutations alter heat-shock gene expression through transcript fragmentation [4].
  • This untimely mRNA degradation accounts for the disproportionate decreases in polypeptide synthesis in prt1 mutant cells [4].

Biological context of PRT1

  • It maps to the right arm of chromosome XV, tightly linked to PRT1, and its sequence matches the sequence of PDE2, encoding the low-Km cAMP phosphodiesterase [5].
  • This protein-synthesis mutation exerts a dna phenotype due to cell-cycle inhibition: prt1 mutations can block the regulatory step of the cell cycle while allowing significant amounts of protein synthesis to continue [6].
  • Isolation and characterization of PRT1, a gene required for the initiation of protein biosynthesis in Saccharomyces cerevisiae [7].
  • Transcript analysis and deletion of the PRT1 5' end revealed that translation of PRT1 mRNA is probably initiated at the second in-frame ATG in the open reading frame [8].
  • Molecular characterization of the yeast PRT1 gene in which mutations affect translation initiation and regulation of cell proliferation [9].

Anatomical context of PRT1

  • This polysome association was further verified by using a conditional allele of essential translation initiation factor PRT1, which markedly decreased polysome association of viral genomic RNA in the presence or absence of an LSM7 mutation [10].
  • Nip1p associates with 40 S ribosomes and the Prt1p subunit of eukaryotic initiation factor 3 and is required for efficient translation initiation [11].

Associations of PRT1 with chemical compounds

  • We purified a polyhistidine-tagged form of Prt1p (His-Prt1p) by Ni2+ affinity and gel filtration chromatography and obtained a complex of approximately 600 kDa composed of six polypeptides whose copurification was completely dependent on the polyhistidine tag on His-Prt1p [12].
  • This response of cessation of cell division is different from the response of cells to an equivalent limitation of protein synthesis using cycloheximide or verrucarin A, which implies that the PRT1 gene product could separately influence both cellular growth via protein synthesis and events in the regulation of cell proliferation [13].
  • Translation initiation factor Prt1 was purified from a ribosomal salt wash fraction of Saccharomyces cerevisiae cells by ammonium sulfate precipitation, DEAE chromatography, phosphocellulose chromatography, sucrose density gradient centrifugation, and non-denaturing polyacrylamide gel electrophoresis [14].
  • However, under conditions in which ribosome biogenesis was inhibited (e.g., inhibition of transcription with thiolutin, inhibition of transcription of ribosomal protein and RNA genes in a sly1-1 mutant at nonpermissive temperature, and inhibition of translation in a conditional prt1 mutant), Nmd3p remained associated with 60S subunits [15].

Other interactions of PRT1


Analytical, diagnostic and therapeutic context of PRT1

  • 2. Southern blot analysis demonstrated that PRT1 is a single copy gene which is transcribed into a 2.3-kilobase RNA [7].
  • Here we report the molecular cloning and characterization of the PRT1 gene from yeast [9].
  • Immunoblotting shows that the 90-kDa subunit corresponds to the product of the PRT1 gene whose mutant form, prt1-1, exhibits destabilization of methionyl-tRNAi binding to 40 S ribosomal subunits. eIF-3, and specifically the 62-kDa subunit, bind to RNA [18].


  1. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. Valásek, L., Nielsen, K.H., Hinnebusch, A.G. EMBO J. (2002) [Pubmed]
  2. A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)Met. Phan, L., Schoenfeld, L.W., Valásek, L., Nielsen, K.H., Hinnebusch, A.G. EMBO J. (2001) [Pubmed]
  3. Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation. Verlhac, M.H., Chen, R.H., Hanachi, P., Hershey, J.W., Derynck, R. EMBO J. (1997) [Pubmed]
  4. Yeast prt1 mutations alter heat-shock gene expression through transcript fragmentation. Barnes, C.A., Singer, R.A., Johnston, G.C. EMBO J. (1993) [Pubmed]
  5. SRA5 encodes the low-Km cyclic AMP phosphodiesterase of Saccharomyces cerevisiae. Wilson, R.B., Tatchell, K. Mol. Cell. Biol. (1988) [Pubmed]
  6. Cell-cycle mutations among the collection of Saccharomyces cerevisiae dna mutants. Evans, D.R., Singer, R.A., Johnston, G.C., Wheals, A.E. FEMS Microbiol. Lett. (1994) [Pubmed]
  7. Isolation and characterization of PRT1, a gene required for the initiation of protein biosynthesis in Saccharomyces cerevisiae. Keierleber, C., Wittekind, M., Qin, S.L., McLaughlin, C.S. Mol. Cell. Biol. (1986) [Pubmed]
  8. Mutational analysis of the Prt1 protein subunit of yeast translation initiation factor 3. Evans, D.R., Rasmussen, C., Hanic-Joyce, P.J., Johnston, G.C., Singer, R.A., Barnes, C.A. Mol. Cell. Biol. (1995) [Pubmed]
  9. Molecular characterization of the yeast PRT1 gene in which mutations affect translation initiation and regulation of cell proliferation. Hanic-Joyce, P.J., Singer, R.A., Johnston, G.C. J. Biol. Chem. (1987) [Pubmed]
  10. Yeast Lsm1p-7p/Pat1p deadenylation-dependent mRNA-decapping factors are required for brome mosaic virus genomic RNA translation. Noueiry, A.O., Diez, J., Falk, S.P., Chen, J., Ahlquist, P. Mol. Cell. Biol. (2003) [Pubmed]
  11. Nip1p associates with 40 S ribosomes and the Prt1p subunit of eukaryotic initiation factor 3 and is required for efficient translation initiation. Greenberg, J.R., Phan, L., Gu, Z., deSilva, A., Apolito, C., Sherman, F., Hinnebusch, A.G., Goldfarb, D.S. J. Biol. Chem. (1998) [Pubmed]
  12. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Phan, L., Zhang, X., Asano, K., Anderson, J., Vornlocher, H.P., Greenberg, J.R., Qin, J., Hinnebusch, A.G. Mol. Cell. Biol. (1998) [Pubmed]
  13. Regulated arrest of cell proliferation mediated by yeast prt1 mutations. Hanic-Joyce, P.J., Johnston, G.C., Singer, R.A. Exp. Cell Res. (1987) [Pubmed]
  14. Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyces cerevisiae. Danaie, P., Wittmer, B., Altmann, M., Trachsel, H. J. Biol. Chem. (1995) [Pubmed]
  15. Nascent 60S ribosomal subunits enter the free pool bound by Nmd3p. Ho, J.H., Kallstrom, G., Johnson, A.W. RNA (2000) [Pubmed]
  16. Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast. Nielsen, K.H., Valásek, L., Sykes, C., Jivotovskaya, A., Hinnebusch, A.G. Mol. Cell. Biol. (2006) [Pubmed]
  17. Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. Asano, K., Phan, L., Anderson, J., Hinnebusch, A.G. J. Biol. Chem. (1998) [Pubmed]
  18. Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein. Naranda, T., MacMillan, S.E., Hershey, J.W. J. Biol. Chem. (1994) [Pubmed]
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