Amino-terminal charge affects the periplasmic accumulation of recombinant heregulin/EGF hybrids exported using the Escherichia coli alkaline phosphatase signal sequence

Protein Expression and Purification

Volumn 10, Issue 3, 1997, Pages 331-339

  Campion, Stephen R ^a   Elsasser, Elizabeth ^a   Chung, Roger ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; TRIXIS;

EID: 0031213695     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0741     Document Type: Article

References (29)

1. Wülfing C., Pluckthun A. Protein folding in the periplasm ofEscherichia coli. Mol. Microbiol. 12:1994;685-692.
2. Missiakas D., Georgopoulos C., Raina S. TheEscherichia coli dsbCxprA. EMBO J. 13:1994;2013-2020.
3. Guilhot C., Jander G., Martin N. L., Beckwith J. Evidence that the pathway of disulfide bond formation inEscherichia coli. Proc. Natl. Acad. Sci. USA. 92:1995;9895-9899.
4. von Heijne. Patterns of amino acids near signal sequence cleavage sites. Eur. J. Biochem. 133:1983;17-21.
5. von Heijne. Analysis of the distribution of charged residues in the N-terminal region of signal sequences: Implications for protein export in prokaryotic and eukaryotic cells. EMBO J. 3:1984;2315-2318.
6. von Heijne. Net N-C charge imbalance may be important for signal sequence function in bacteria. J. Mol. Biol. 192:1986;287-290.
7. Li P., Beckwith J., Inouye H. Alteration of the amino-terminus of the mature sequence of a periplasmic protein can severely affect protein export inEscherichia coli. Proc. Natl. Acad. Sci. USA. 85:1988;7685-7689.
8. Yamane K., Mizushima S. Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane ofEscherichia coli. J. Biol. Chem. 263:1988;19690-19696.
9. Summers R. G., Harris C. R., Knowles J. R. A conservative substitution, arginine for lysine, abolishes export of hybrid protein inEscherichia coli. J. Biol. Chem. 264:1989;20082-20088.
10. MacIntyre S., Eschbach M.-L., Mutschler B. Export incompatability of N-terminal basic residues in a mature polypeptide ofEscherichia coli. Mol. Gen. Genet. 221:1990;466-474.
11. Vlasuk G. P., Inouye S., Ito H., Itakura K., Inouye M. Effects of complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein inEscherichia coli. J. Biol. Chem. 258:1983;7141-7148.
12. Iiona T., Takahashi M., Sako T. Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane ofEscherichia coli. J. Biol. Chem. 262:1987;7412-7417.
13. Boyd D., Beckwith J. The role of charged amino acids in the localization of secreted and membrane proteins. Cell. 62:1990;1031-1033.
14. Puziss J. W., Fikes J. D., Bassford P. J. Jr. Analysis of mutational alterations in the hydrophobic segment of the maltose-binding protein signal peptide. J. Bacteriol. 171:1989;2303-2311.
15. Puziss J. W., Strobel S. M., Bassford P. J. Jr. Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core inEscherichia coliprl. J. Bacteriol. 174:1992;92-101.
16. Chou M. M., Kendall D. A. Polymeric sequences reveal a functional inter-relationship between hydrophobicity and length of signal peptides. J. Biol. Chem. 265:1990;2873-2880.
17. Rusch S. L., Kendall D. A. Transport of an export-defective protein by a highly hydrophobic signal peptide. J. Biol. Chem. 269:1994;1243-1248.
18. Engler D. A, Matsunami R. K., Campion S. K., Stringer C. D., Stevens A., Niyogi S. K. Cloning of authentic human epidermal growth factor as a bacterial secretory protein and its initial structure function analysis by site-directed mutagenesis. J. Biol. Chem. 263:1988;12384-12390.
19. Campion S. R., Matsunami R. K., Engler D. A., Niyogi S. K. Biochemical properties of site-directed mutants of human epidermal growth factor: Importance of solvent-exposed residues of the amino-terminal domain in receptor binding. Biochemistry. 29:1990;9988-9993.
20. erbB2. Science. 256:1992;1205-1210.
21. Barbacci E. G., Guarino B. C., Stroh J. G., Singleton D. H., Rosnack K. J., Moyer J. D., Andrews G. C. The structural basis for the specificity of epidermal growth factor and heregulin binding. J. Biol. Chem. 270:1995;9585-9589.
22. Hanahan D. Techniques for transformation ofE. coli. DNA Cloning. 1985;IRL Press, Oxford. p. 109-135.
23. Laemmli U. K. Cleavage of the structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
24. Campion S. R., Biamonti C., Montelione G. T., Niyogi S. K. The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. Protein Eng. 6:1993;651-659.
25. Economou A., Pogliano J. A., Beckwith J., Oliver D. B., Wickner W. SecAsecYEGsecDsecF. Cell. 83:1995;1171-1181.
26. Kim Y. J., Rajapandi T., Oliver D. SecAE. coli. Cell. 78:1994;845-853.
27. Rajapandi T., Oliver D. Carboxy-terminal region ofEscherichia coli SecA. Biochem. Biophys. Res. Commun. 200:1994;1477-1483.
28. Pohlschroder M., Murphy C., Beckwith J. In vivoSecESecY,Escherichia coli. J. Biol. Chem. 271:1996;19908-19914.
29. Blight M. A., Chervaux C., Holland I. B. Protein secretion pathways inEscherichia coli. Curr. Opin. Biotechnol. 5:1994;468-474.