Single-Amino-Acid Substitutions within the Signal Sequence of Yeast Prepro-α-Factor Affect Membrane Translocation

LITERATURE CITED

• Alber, T., and G. Kawasaki. 1982. Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae. J. Mol. Appl. Genet. 1:419–434.
   PubMedGoogle Scholar
• Allison, D. S., and G. Schatz. 1986. Artificial mitochondrial presequences. Proc. Natl. Acad. Sci. USA 83:9011–9015.
   PubMedGoogle Scholar
• Ammerer, G. 1983. Expression of genes in yeast using the ADCI promoter. Methods Enzymol. 101:192–201.
   PubMed Web of Science ®Google Scholar
• Benson, S. A., Μ. N. Hall, and T. J. Silhavy. 1985. Genetic analysis of protein export in Escherichia coli K12. Annu. Rev. Biochem. 54:101–134.
   PubMed Web of Science ®Google Scholar
• Blachly-Dyson, E., and T. H. Stevens. 1987. Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal sequence. J. Cell Biol. 104:1183–1191.
   PubMed Web of Science ®Google Scholar
• Biobel, G., and B. Dobberstein. 1975. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67:835–851.
   PubMedGoogle Scholar
• Böhni, P. C., G. Daum, and G. Schatz. 1983. Import of proteins into mitochondria: partial purification of a matrix-located protease involved in cleavage of mitochondrial precursor polypeptides. J. Biol. Chem. 258:4937–4943.
   PubMedGoogle Scholar
• Briggs, Μ. S., D. G. Cornell, R. A. Dluhy, and L. Μ. Gierasch. 1986. Conformations of signal peptides induced by lipids suggest initial steps in protein export. Science 233:206–208.
   PubMed Web of Science ®Google Scholar
• Briggs, Μ. S., L. Μ. Gierasch, A. Zlotnick, J. D. Lear, and W. F. DeGrado. 1985. In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides. Science 228:1096–1099.
   PubMedGoogle Scholar
• Brown, P. A., H. O. Halvorson, P. Raney, and D. Perlman. 1984. Conformational alterations in the proximal portion of the yeast invertase signal peptide do not block secretion. Mol. Gen. Genet. 197:351–357.
   PubMedGoogle Scholar
• Deshaies, R. J., and R. Schekman. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105:633–645.
   PubMedGoogle Scholar
• Dowhan, W., C. R. Bibus, and G. Schatz. 1985. The cytoplasmi-cally-made subunit IV is necessary for assembly of cytochrome c oxidase in yeast. EMBO J. 4:179–184.
   PubMedGoogle Scholar
• Emr, S. D., and T. J. Silhavy. 1983. Importance of secondary structure in the signal sequence for protein secretion. Proc. Natl. Acad. Sci. USA 80:4599–4603.
   PubMed Web of Science ®Google Scholar
• Gasser, S. Μ., G. Daum, and G. Schatz. 1982. Import of proteins into mitochondria: energy-dependent uptake of precursors by isolated mitochondria. J. Biol. Chem. 257:13034–13041.
   PubMed Web of Science ®Google Scholar
• Hansen, W., P. D. Garcia, and P. Walter. 1986. In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-α-factor. Cell 45:397–406.
   PubMedGoogle Scholar
• Hurt, E. C., D. S. Allison, U. Müller, and G. Schatz. 1987. Amino-terminal deletions in the presequence of an imported mitochondrial protein block the targeting function and proteolytic cleavage at the carboxy terminus. J. Biol. Chem. 262:1420–1424.
   PubMedGoogle Scholar
• Hurt, E. C., B. Pesold-Hurt, and G. Schatz. 1984. The aminoterminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix. EMBO J. 3:3149–3156.
   PubMedGoogle Scholar
• Hurt, E. C., B. Pesold-Hurt, K. Suda, W. Oppliger, and G. Schatz. 1985. The first twelve amino acids (less than half of the pre-sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix. EMBO J. 4:2061–2068.
   PubMed Web of Science ®Google Scholar
• Ibrahimi, I., and R. Gentz. 1987. A functional interaction between the signal peptide and the translation apparatus is detected by the use of a single point mutation which blocks translocation across mammalian endoplasmic reticulum. J. Biol. Chem. 262:10189–10194.
   PubMedGoogle Scholar
• Ito, H., Y. Kukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Julius, D., L. Blair, A. Brake, G. Sprague, and J. Thorner. 1983. Yeast a factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell 32:839–852.
   PubMed Web of Science ®Google Scholar
• Kaiser, C. A., and D. Botstein. 1986. Secretion-defective mutations in the signal sequence for Saccharomyces cerevisiae invertase. Mol. Cell. Biol. 6:2382–2391.
   PubMed Web of Science ®Google Scholar
• Kaiser, C. A., D. Preuss, P. Grisafi, and D. Botstein. 1987. Many random sequences functionally replace the secretion signal sequence of yeast invertase. Science 235:312–317.
   PubMed Web of Science ®Google Scholar
• Kurjan, J. 1985. α-Factor structural gene mutations in Saccharomyces cerevisiae: effects on α-factor production and mating. Mol. Cell. Biol. 5:787–796.
   PubMed Web of Science ®Google Scholar
• Kurjan, J., and I. Herskowitz. 1982. Structure of a yeast pheromone gene (MFα): A putative α-factor precursor contains four tandem copies of mature α-factor. Cell 30:933–943.
   PubMed Web of Science ®Google Scholar
• Maarse, A. C., A. P. G. Μ. Van Loon, H. Riezman, I. Gregor, G. Schatz, and L. A. Grivell. 1984. Subunit IV of yeast cytochrome c oxidase: cloning and nucleotide sequencing and partial amino acid sequencing of the mature protein. EMBO J. 3:2831–2837.
   PubMedGoogle Scholar
• Maxam, A. Μ., and W. Gilbert. 1980. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65:499–560.
   PubMedGoogle Scholar
• Michaelis, S., and J. Beckwith. 1982. Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu. Rev. Microbiol. 36:435–465.
   PubMed Web of Science ®Google Scholar
• Milstein, C., G. G. Brownlee, T. Μ. Harrison, and Μ. D. Mathews. 1972. A possible precursor of immunoglobulin light chains. Nature New Biol. 239:117–120.
   PubMedGoogle Scholar
• Müller, Μ., I. Ibrahimi, C. N. Chang, P. Walter, and G. Blobel. 1982. A bacterial secretory protein requires signal recognition particle for translocation across mammalian endoplasmic reticulum. J. Biol. Chem. 257:11860–11863.
   PubMedGoogle Scholar
• Myers, R. Μ., L. S. Lerman, and T. Maniatis. 1985. A general method for saturation mutagenesis of cloned DNA fragments. Science 229:242–247.
   PubMed Web of Science ®Google Scholar
• Perlman, D., P. Raney, and H. O. Halvorson. 1986. Mutations affecting the signal sequence alter synthesis and secretion of yeast invertase. Proc. Natl. Acad. Sci. USA 83:5033–5037.
   PubMedGoogle Scholar
• Pilgrim, D., and E. T. Young. 1987. Primary structure requirements for correct sorting of the yeast mitochondrial protein ADH III to the yeast mitochondrial matrix space. Mol. Cell. Biol. 7:294–304.
   PubMed Web of Science ®Google Scholar
• Roise, D., S. J. Horvath, J. Μ. Tomich, J. H. Richards, and G. Schatz. 1986. A chemically synthesized presequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EMBO J. 5:1327–1334.
   PubMed Web of Science ®Google Scholar
• Rothblatt, J. A., and D. I. Meyer. 1986. Secretion in yeast: reconstitution of the translocation and glycosylation of α-factor and invertase in a homologous cell-free system. Cell 44:619–628.
   PubMedGoogle Scholar
• Schauer, L., S. Emr, C. Gross, and R. Schekman. 1985. Invertase signal and mature sequence substitutions that delay inter-compartmental transport of active enzyme. J. Cell Biol. 100:1664–1675.
   PubMedGoogle Scholar
• Shaw, K. J., and Μ. V. Olson. 1984. Effects of altered 5′-flanking sequences on the in vivo expression of a Saccharomyces cerevisiae tRNATyr gene. Mol. Cell. Biol. 4:657–665.
   PubMed Web of Science ®Google Scholar
• Silve, S., Μ. Monod, A. Hinnen, and R. Haguenauer-Tsapis. 1987. The yeast acid phosphatase can enter the secretory pathway without its N-terminal signal sequence. Mol. Cell. Biol. 7:3306–3314.
   PubMedGoogle Scholar
• Suissa, Μ. 1983. Spectrophotometric quantitation of silver grains eluted from autoradiograms. Anal. Biochem. 133:511–514.
   PubMed Web of Science ®Google Scholar
• Talmadge, K., S. Stahl, and W. Gilbert. 1980. Eucaryotic signal sequence transports insulin antigen in Escherichia coli. Proc. Natl. Acad. Sci. USA 77:3369–3373.
   PubMed Web of Science ®Google Scholar
• Van Loon, A. P. G. Μ., and E. T. Young. 1986. Intracellular sorting of alcohol dehydrogenase isoenzymes in yeast: a cytosolic location reflects absence of an amino-terminal targeting sequence for the mitochondria. EMBO J. 5:161–165.
   PubMed Web of Science ®Google Scholar
• Von Heijne, G. 1985. Signal sequences: the limits of variation. J. Mol. Biol. 184:99–105.
   PubMed Web of Science ®Google Scholar
• Walter, P. 1987. Two receptors act sequentially. Nature (London) 328:763–764.
   PubMedGoogle Scholar
• Walter, P., and G. Blobel. 1980. Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 77:7112–7116.
   PubMed Web of Science ®Google Scholar
• Waters, Μ. G., and G. Blobel. 1986. Secretory protein translocation in a yeast cell-free system can occur post-translationally and requires ATP hydrolysis. J. Cell Biol. 102:1543–1550.
   PubMedGoogle Scholar
• Waters, Μ. G., W. J. Chirico, and G. Blobel. 1986. Protein translocation across the yeast microsomal membrane is stimulated by a soluble factor. J. Cell Biol. 103:2629–2636.
   PubMedGoogle Scholar
• Wickner, W. 1979. The assembly of proteins into biological membranes: the membrane trigger hypothesis. Annu. Rev. Biochem. 48:23–45.
   PubMed Web of Science ®Google Scholar
• Wiedmann, Μ., T. V. Kurzchalia, E. Hartmann, and T. A. Rapoport. 1987. A signal sequence receptor in the endoplasmic reticulum membrane. Nature (London) 328:830–833.
   PubMed Web of Science ®Google Scholar