Processing of Escherichia coli alkaline phosphatase: Sequence requirements and possible conformations of the -6 to -4 region of the signal peptide

Journal of Biological Chemistry

Volumn 277, Issue 52, 2002, Pages 50396-50402

  Kajava, Andrey V ^a,d   Zolov, Sergey N ^b   Pyatkov, Konstantin I ^c   Kalinin, Andrey E ^b,e   Nesmeyanova, Marina A ^b,d  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b SKRYABIN INSTITUTE OF BIOCHEMISTRY AND PHYSIOLOGY OF MICROORGANISMS   (Russian Federation)

^c INSTITUTE OF CELL BIOPHYSICS   (Russian Federation)

^d Centre National de la Recherche Scientifique   (France)

^e NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; HYDROPHOBICITY; PHOSPHATES; SIGNALING; SUBSTRATES;

ALKALINES;

ESCHERICHIA COLI;

ALKALINE PHOSPHATASE; BETA LACTAM; ISOLEUCINE; LEUCINE; PROLINE; SERINE; SIGNAL PEPTIDASE; TYROSINE; VALINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ESCHERICHIA COLI; HYDROPHOBICITY; MUTATIONAL ANALYSIS; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN PROCESSING; PROTEIN TRANSPORT;

ALKALINE PHOSPHATASE; AMINO ACID SEQUENCE; BASE SEQUENCE; ESCHERICHIA COLI; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0037184936     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M205781200     Document Type: Article

References (54)

1. Dalbey, R. E., and Von Heijne, G. (1992) Trends Biochem. Sci 17, 474-478
2. Perlman, D., and Halvorson, H. O. (1983) J. Mol. Biol. 167, 391-409
3. von Heijne, G. (1985) J. Mol. Biol. 184, 99-105
4. Summers, R. G., and Knowles, J. R. (1989) J. Biol. Chem. 264, 20074-20081
5. Kuhn, A., Kiefer, D., Kohne, C., Zhu, H. Y., Tschantz, W. R., and Dalbey, R. E. (1994) Eur. J. Biochem. 226, 891-897
6. Kajava, A. V., Zolov, S. N., Kalinin, A. E., and Nesmeyanova, M. A. (2000) J. Bacteriol. 182, 2163-2169
7. Fekkes, P., and Driessen, A. J. (1999) Microbiol. Mol. Biol. Rev. 63, 161-173
8. Nesmeyanova, M. A., and Bogdanov, M. V. (1989) FEBS Lett. 257, 203-207
9. de Vrije, T., de Swart, R. L., Dowhan, W., Tommassen, J., and de Kruijff, B. (1988) Nature 334, 173-175
10. Killian, J. A., de Jong, A. M., Bijvelt, J., Verkleij, A. J., and de Kruijff, B. (1990) EMBO J. 9, 815-819
11. Nesmeyanova, M. A., Karamyshev, A. L., Karamysheva, Z. N., Kalinin, A. E., Ksenzenko, V. N., and Kajava, A. V. (1997) FEBS Lett. 403, 203-207
12. Van Voorst, F., and De Kruijff, B. (2000) Biochem. J. 347, 601-612
13. Chou, M. M., and Kendall, D. A. (1990) J. Biol. Chem. 265, 2873-2880
14. Lill, R., Dowhan, W., and Wickner, W. (1990) Cell 60, 271-280
15. Pugsley, A. P. (1993) Microbiol. Rev. 57, 50-108
16. Von Heijne, G. (1986) J. Mol. Biol. 192, 287-290
17. Zimmermann, R., Watts, C., and Wickner, W. (1982) J. Biol. Chem. 257, 6529-6536
18. Dalbey, R. E., Lively, M. O., Bron, S., and van Dijl, J. M. (1997) Protein Sci. 6, 1129-1138
19. Paetzel, M., Dalbey, R. E., and Strynadka, N. C. (1998) Nature 396, 186-190
20. Izard, J. W., and Kendall, D. A. (1994) Mol. Microbiol. 13, 765-773
21. Plath, K., Mothes, W., Wilkinson, B. M., Stirling, C. J., and Rapoport, T. A. (1998) Cell 94, 795-807
22. Paetzel, M., Dalbey, R. E., and Strynadka, N. C. (2002) J. Biol. Chem. 277, 9512-9519
23. Koshland, D., Sauer, R. T., and Botstein, D. (1982) Cell 30, 903-914
24. Barkocy-Gallagher, G. A., Cannon, J. G., and Bassford, P. J., Jr. (1994) J. Biol. Chem. 269, 13609-13613
25. Laforet, G. A., and Kendall, D. A. (1991) J. Biol. Chem. 266, 1326-1334
26. Chou, P. Y., and Fasman, G. D. (1979) Biophys. J. 26, 367-373
27. Rosenblatt, M., Beaudette, N. V., and Fasman, G. D. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 3983-3987
28. Shen, L. M., Lee, J. I., Cheng, S. Y., Jutte, H., Kuhn, A., and Dalbey, R. E. (1991) Biochemistry 30, 11775-11781
29. Karamyshev, A. L., Karamysheva, Z. N., Kajava, A. V., Ksenzenko, V. N., and Nesmeyanova, M. A. (1998) J. Mol. Biol. 277, 859-870
30. Palzkill, T., Le, Q. Q., Wong, A., and Botstein, D. (1994) J. Bacteriol. 176, 563-568
31. Kadonaga, J. T., Pluckthun, A., and Knowles, J. R. (1985) J. Biol. Chem. 260, 16192-16199
32. Niviere, V., Wong, S. L., and Voordouw, G. (1992) J. Gen. Microbiol. 138, 2173-2183
33. Nielsen, H., Engelbrecht, J., von Heijne, G., and Brunak, S. (1996) Proteins 24, 165-177
34. Bachmann, B. J. (1987) in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F. C., ed), American Society for Microbiology, Washington, D. C.
35. Zaitsev, E. N., Zaitseva, E. M., Bakhlanova, I. V., Gorelov, V. N., and Kuz'min, N. P. (1986) Genetika 22, 2721-2727
36. Kleina, L. G., Masson, J. M., Normanly, J., Abelson, J., and Miller, J. H. (1990) J. Mol. Biol. 213, 705-717
37. Inouye, H., Michaelis, S., Wright, A., and Beckwith, J. (1981) J. Bacteriol. 146, 668-675
38. Torriani, A. (1966) in Procedures in Nucleic Acid Research (Cantoni, G. L., and Davis, R., eds), pp. 224-234, Harper and Row, New York
39. Kalinin, A. E., Mikhaleva, N. I., Karamyshev, A. L., Karamysheva, Z. N., and Nesmeyanova, M. A. (1999) Biochemistry-Russia 64, 1021-1029
40. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, New York
41. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U. S. A. 74, 5463-5467
42. Davis, B. J. (1964) Ann. N. Y. Acad. Sci. 121, 404-427
43. Lojda, Z., Grossrau, R., and Schibler, T. H. (1979) Enzyme Histochemistry: A Laboratory Manual., Springer-Verlag, Berlin, Germany
44. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
45. Dayring, H. E., Tramonato, A., Sprang, S. R., and Fletterick, R. J. (1986) J. Mol. Graphics 4, 82-87
46. Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., and Karplus, M. (1983) J. Computat. Chem. 4, 187-217
47. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
48. Fauchere, J., and Pliska, V. (1983) Eur. J. Med. Chem. 18, 369-375
49. Michaelis, S., Inouye, H., Oliver, D., and Beckwith, J. (1983) J. Bacteriol. 154, 366-374
50. Boyd, D., Guan, C.-D., Willard, S., Wright, W., Strauch, K., and Beckwith, J. (1987) in Phosphate Metabolism and Cellular Regulation in Microorganisms (Torriani-Gorini, A., Rothman, F. G., Silver, S., Wright, A. & Yagil, E., eds) pp. 89-93, American Society for Microbiology, Washington, D. C.
51. Karamyshev, A. L., Kalinin, A. E., Tsfasman, I. M., Ksenzenko, V. N., and Nesmeianova, M. A. (1994) Mol. Biol. (Mosk) 28, 362-373
52. Luo, Y., Pfuetzner, R. A., Mosimann, S., Paetzel, M., Frey, E. A., Cherney, M., Kim, B., Little, J. W., and Strynadka, N. C. (2001) Cell 106, 585-594
53. Martoglio, B., Hofmann, M. W., Brunner, J., and Dobberstein, B. (1995) Cell 81, 207-214
54. Venable, R. M., Zhang, Y., Hardy, B. J., and Pastor, R. W. (1993) Science 262, 223-226