The Evolutionarily Conserved Eukaryotic Arginine Attenuator Peptide Regulates the Movement of Ribosomes That Have Translated It

REFERENCES

• Baek, J.-M., and C. M. Kenerley 1998. The arg2 gene of Trichoderma virens: cloning and development of a homologous transformation system. Fungal Genet. Biol. 23: 34–44.
   PubMedGoogle Scholar
• Cao, J., and A. P. Geballe 1998. Ribosomal release without peptidyl tRNA hydrolysis at translation termination in a eukaryotic system. RNA 4: 181–188.
   PubMedGoogle Scholar
• Crabeel, M., R. LaValle, and N. Glansdorff 1990. Arginine-specific repression in Saccharomyces cerevisiae: kinetic data on ARG1 and ARG3 mRNA transcription and stability support a transcriptional control mechanism. Mol. Cell. Biol. 10: 1226–1233.
   PubMedGoogle Scholar
• Davis, R. H. 1986. Compartmental and regulatory mechanisms in the arginine pathways of Neurospora crassa and Saccharomyces cerevisiae. Microbiol. Rev. 50: 280–313.
   PubMedGoogle Scholar
• Delbecq, P., M. Werner, A. Feller, R. K. Filipkowski, F. Messenguy, and A. Piérard 1994. A segment of mRNA encoding the leader peptide of the CPA1 gene confers repression by arginine on a heterologous yeast gene transcript. Mol. Cell. Biol. 14: 2378–2390.
   PubMed Web of Science ®Google Scholar
• Edelmann, S. E., and C. Staben 1994. A statistical analysis of sequence features within genes from Neurospora crassa. Exp. Mycol. 18: 70–81.
   Google Scholar
• Farabaugh, P. J. 1996. Programmed translational frameshifting. Microbiol. Rev. 60: 103–134.
   PubMedGoogle Scholar
• Federov, A. N., and T. O. Baldwin 1998. Protein folding and assembly in a cell-free expression system. Methods Enzymol. 290: 1–17.
   PubMedGoogle Scholar
• Freitag, M., N. Dighde, and M. S. Sachs 1996. A UV-induced mutation that affects translational regulation of the Neurospora arg-2 gene. Genetics 142: 117–127.
   PubMedGoogle Scholar
• Hinnebusch, A. G. 1997. Translational regulation of yeast GCN4: a window on factors that control initiator-tRNA binding to the ribosome. J. Biol. Chem. 272: 21661–21664.
   PubMed Web of Science ®Google Scholar
• Képès, F. 1996. The “+70 pause”: hypothesis of a translational control of membrane protein assembly. J. Mol. Biol. 262: 77–86.
   PubMed Web of Science ®Google Scholar
• Koloteva, N., P. P. Muller, and J. E. McCarthy 1997. The position dependence of translational regulation via RNA-RNA and RNA-protein interactions in the 5′-untranslated region of eukaryotic mRNA is a function of the thermodynamic competence of 40 S ribosomes in translational initiation. J. Biol. Chem. 272: 16531–16539.
   PubMedGoogle Scholar
• Komar, A. A., and R. Jaenicke 1995. Kinetics of translation of γ B crystallin and its circularly permutated variant in an in vitro cell-free system: possible relations to codon distribution and protein folding. FEBS Lett. 376: 195–198.
   PubMed Web of Science ®Google Scholar
• Landick, R., C. L. J. Turnbough, and C. Yanofsky Transcription attenuation Escherichia coli and Salmonella: cellular and molecular biology In: Neidhardt, F. C., Curtiss, R.III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Maasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger119961263–1286ASM Press, Washington, D.C.
   Google Scholar
• Larsen, B., J. Peden, S. Matsufuji, T. Matsufuji, K. Brady, R. Maldonado, N. M. Wills, O. Fayet, J. F. Atkins, and R. F. Gesteland 1995. Upstream stimulators for recoding. Biochem. Cell Biol. 73: 1123–1129.
   PubMedGoogle Scholar
• Liao, S., J. Lin, H. Do, and A. E. Johnson 1997. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90: 31–41.
   PubMedGoogle Scholar
• Lovett, P. S., and E. J. Rogers 1996. Ribosome regulation by the nascent peptide. Microbiol. Rev. 60: 366–385.
   PubMedGoogle Scholar
• Luo, Z., M. Freitag, and M. S. Sachs 1995. Translational regulation in response to changes in amino acid availability in Neurospora crassa. Mol. Cell. Biol. 15: 5235–5245.
   PubMedGoogle Scholar
• Luo, Z., and M. S. Sachs 1996. Role of an upstream open reading frame in mediating arginine-specific translational control in Neurospora crassa. J. Bacteriol. 178: 2172–2177.
   PubMedGoogle Scholar
• Orbach, M. J., M. S. Sachs, and C. Yanofsky 1990. The Neurospora crassa arg-2 locus: structure and expression of the gene encoding the small subunit of arginine-specific carbamoyl phosphate synthetase. J. Biol. Chem. 265: 10981–10987.
   PubMed Web of Science ®Google Scholar
• Shen, W.-C., and D. J. Ebbole 1997. Cross-pathway and pathway-specific control of amino acid biosynthesis in Magnaporthe grisea. Fungal Genet. Biol. 21: 40–49.
   Google Scholar
• Srb, A. M., and N. H. Horowitz 1944. The ornithine cycle in Neurospora and its genetic control. J. Biol. Chem. 154: 129–139.
   Google Scholar
• Thanaraj, T. A., and P. Argos 1996. Ribosome-mediated translational pause and protein domain organization. Protein Sci. 5: 1594–1612.
   PubMed Web of Science ®Google Scholar
• Walter, P., and A. E. Johnson 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell. Biol. 10: 87–119.
   PubMedGoogle Scholar
• Wang, Z., and M. S. Sachs 1997. Arginine-specific regulation mediated by the Neurospora crassa arg-2 upstream open reading frame in a homologous, cell-free in vitro translation system. J. Biol. Chem. 272: 255–261.
   PubMedGoogle Scholar
• Wang, Z., and M. S. Sachs 1997. Ribosome stalling is responsible for arginine-specific translational attenuation in Neurospora crassa. Mol. Cell. Biol. 17: 4904–4913.
   PubMedGoogle Scholar
• Werner, M., A. Feller, F. Messenguy, and A. Piérard 1987. The leader peptide of yeast CPA1 is essential for the translational repression of its expression. Cell 49: 805–813.
   PubMed Web of Science ®Google Scholar