Effects of signal peptide mutations on processing of Bacillus stearothermophilus α-amylase in Escherichia coli

References

1. Barkocy-Gallagher G. A., Bassford P. J. Jr. 1992; Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo . J Biol Chem 267:1231–1238
   [Google Scholar]
2. Barthelemy I., De Buitrago G. G., Carreiro C., Roncal F., Perez-Aranda A., Marquez G., Barbero J. L. 1993; Production and secretion of human interleukin 6 into the periplasm of Eschericia coli : efficient processing of N-terminal variants of hIL6 by the E coli signal peptidase. J Biotechnol 27:307–316
   [Google Scholar]
3. Benson S. A., Hall M. N., Rasmussen B. A. 1987; Signal sequence mutations that alter coupling of secretion and translation of an Escherichia coli outer membrane protein . J Bacteriol 169:4686–4691
   [Google Scholar]
4. Boyer H. W., Roulland-Dussoix D. 1969; A complementation analysis of the restriction and modification of DNA in Escherichia coli . J Mol Biol 41:459–472
   [Google Scholar]
5. Chou P. Y., Fasman G. D. 1978; Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol 47:45–148
   [Google Scholar]
6. Cornelis P., Digneffe C., Willemot K. 1982; Cloning and expression of a Bacillus coagulans amylase gene in Escherichia coli . Mol & Gen Genet 186:507–511
   [Google Scholar]
7. Dev I. K., Ray P. H, Novak P. 1990; Minimum substrate sequence for signal peptidase I of Escherichia coli . J Biol Chem 265:20069–20072
   [Google Scholar]
8. Devereux J., Haeberli P., Smithies O. 1984; A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387–395
   [Google Scholar]
9. van DijI J. M., De Jong A., Smith H., Bron S., Venema G. 1991; Non-functional expression of Escherichia coli signal peptidase I in Bacillus suhtilis . J Gen Microbiol 137:2073–2083
   [Google Scholar]
10. von Heijne G. 1985; Signal sequences The limits of variation. J Mol Biol 184:99–105
    [Google Scholar]
11. von Heijne G. 1986; A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14:4683–4690
    [Google Scholar]
12. von Heijne G., Abrahmsen L. 1989; Species-specific variation in signal peptide design Implications for protein secretion in foreign hosts. FEBS Lett 244:439–446
    [Google Scholar]
13. Ito K., Bassford P. J., Jr & Beckwith J. R. 1981; Protein localization in Escherichia coli: is there a common step in the secretion of periplasmic and outer-membrane proteins?. Cell 24:707–717
    [Google Scholar]
14. Kadonaga J. T., Plückthun A., Knowles J. R. 1985; Signal sequence mutants of β-lactamase. J Biol Chem 260:16192–16199
    [Google Scholar]
15. Kunkel T. A. 1985; Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82:488–492
    [Google Scholar]
16. Kyte J., Doolittle R. F. 1982; A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105–132
    [Google Scholar]
17. Nilsson I., von Heijne G. 1991; A de novo designed signal peptide cleavage casette functions in vivo . J Biol Chem 266:3408–3410
    [Google Scholar]
18. Puziss J. W., Strobel S. M. , Bassford P. J. Jr. 1992; Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Eschericia coli cells harboring prl suppressor mutations. J Bacteriol 174:92–101
    [Google Scholar]
19. Sakakibara Y., Tsutsumi K., Nakamura K., Yamane K. 1993; Structural requirements of Bacillus subtilis α-amylase signal peptide for efficient processing: in vivo pulse-chase experiments with mutant signal peptides. J Bacteriol 175:4203–4212
    [Google Scholar]
20. Sambrook J., Fritsch E. F., Maniatis T. 1989 Molecular Cloning: a Laboratov Manual 2nd edn Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
21. Sanger F., Nicklen S., Coulson A. R. 1977; DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74:5463–5467
    [Google Scholar]
22. Saunders C. W., Pedroni J. A., Monahan P. M. 1991; Optimization of the signal-sequence cleavage site for secretion from Bacillus subtilis of a 34-amino acid fragment of human parathyroid hormone. Gene 102:277–282
    [Google Scholar]
23. Shen L. M., Lee J.-I., Cheng S., Jutte H., Kuhn A., Dalbey R. E. 1991; Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the Ml3 procoat protein by the Escherichia coli leader peptidase. Biochemistry 30:11775–11781
    [Google Scholar]
24. Suominen I., Karp M., Lautamo J., Knowles J., Mantsaick P. 1987a Thermostable α-amylase of Bacillus stearothermophilus: cloning, expression, and secretion by Escherichia coli . In Extracellular Enzymes of Microorganisms Chaloupka J., Krumphanzl V. pp New York: Plenum Press;129–137
    [Google Scholar]
25. Suominen I., Karp M., Lähde M., Kopio A., Glumoff T., Meyer P., Mäntsäiä P. 1987b; Extracellular production of cloned α-amylase by Escherichia coli. Gene 33:165–176
    [Google Scholar]
26. Suominen I., Käpylä J., Tilgmann C., Glumoff V., Mäntsäiä P. 1988; Suppression of growth defects of α-amylase secreting Escherichia coli by signal sequence fusion. FEMS Microbiol Lett 55:3–8
    [Google Scholar]
27. Vieira J., Messing J. 1982; The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259–268
    [Google Scholar]
28. Vihinen M., Mäntsäiä P. 1990; Characterization of a thermo-stable Bacillus stearothermophilus α-amylase. Biotechnol Appl Biochem:427–435
    [Google Scholar]
29. Vihinen M., Ollikka P., Niskanen J., Meyer P., Suominen I., Karp M., Holm L., Knowles J., Mäntsäiä P. 1990; Site-directed mutagenesis of a thermostable α-amylase from Bacillus stearo-thermophilus: putative role of three conserved residues. J Biochem 107:267–272
    [Google Scholar]
30. Watson M. E. E. 1984; Compilation of published signal sequences. Nucleic Acids Res 12:5145–5164
    [Google Scholar]
31. Wolfe P. B., Wickner W. 1984; Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins. Cell 36:1067–1072
    [Google Scholar]
32. Yanisch-Perron C, Vieira J., Messing J. 1985; Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors. Gene 33:103–119
    [Google Scholar]
33. Zagursky R. J., Berman M. L., Baumeister K., Lomax N. 1985; Rapid and easy sequencing of large linear double stranded DNA and supercoiled plasmid DNA. Gene Anal Tech 2:89–94
    [Google Scholar]