FtsH-dependent processing of RNase colicins d and e3 means that only the cytotoxic domains are imported into the cytoplasm

Journal of Biological Chemistry

Volumn 286, Issue 33, 2011, Pages 29397-29407

  Chauleau, Mathieu ^a   Mora, Liliana ^a   Serba, Justyna ^a   De Zamaroczy, Miklos ^a  

^a INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL PEPTIDE; CATALYTIC DOMAINS; COGNATE IMMUNITY PROTEINS; COLICINS; CYTOTOXIC; ENDOPROTEOLYTIC CLEAVAGE; IN-VITRO; IN-VIVO; INNER MEMBRANES; NUCLEASE COLICINS; OUTER MEMBRANE; PROCESSING STEPS; PROTEIN PROCESSING; SIGNAL PEPTIDASE;

ASSOCIATION REACTIONS; BACTERIOLOGY; CELLS; MACHINERY;

CYTOLOGY;

BACTERIAL PROTEIN; COLICIN; COLICIN D; COLICIN E3; OUTER MEMBRANE PROTEIN; PEPTIDASE; PEPTIDASE LEPB; PROTEIN FTSH; PROTEIN TOL; PROTEIN TONB; RIBONUCLEASE; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; CYTOTOXICITY; ENZYME ACTIVITY; ESCHERICHIA COLI; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION;

ATP-DEPENDENT PROTEASES; BACTERIAL OUTER MEMBRANE PROTEINS; CARRIER PROTEINS; COLICINS; CYTOPLASM; ESCHERICHIA COLI K12; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; PROTEIN TRANSPORT; RECEPTORS, CELL SURFACE; RIBONUCLEASES; SERINE ENDOPEPTIDASES;

BACTERIA (MICROORGANISMS);

EID: 80051681504     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.242354     Document Type: Article

References (71)

1. Tomita, K., Ogawa, T., Uozumi, T., Watanabe, K., and Masaki, H. (2000) Proc. Natl. Acad. Sci. U.S.A. 97, 8278-8283
2. Bowman, C. M., Dahlberg, J. E., Ikemura, T., Konisky, J., and Nomura, M. (1971) Proc. Natl. Acad. Sci. U.S.A. 68, 964-968
3. Braun, V., Pilsl, H., and Gross, P. (1994) Arch. Microbiol. 161, 199-206
4. James, R., Kleanthous, C., and Moore, G. R. (1996) Microbiology 142, 1569-1580
5. Benedetti, H., Frenette, M., Baty, D., Knibiehler, M., Pattus, F., and Lazdunski, C. (1991) J. Mol. Biol. 217, 429-439
6. Braun, V., Patzer, S. I., and Hantke, K. (2002) Biochimie 84, 365-380
7. Mora, L., Klepsch, M., Buckingham, R. H., Heurgué-Hamard, V., Kervestin, S., and de Zamaroczy, M. (2008) J. Biol. Chem. 283, 4993-5003
8. Roos, U., Harkness, R. E., and Braun, V. (1989) Mol. Microbiol. 3, 891-902
9. de Zamaroczy, M., and Chauleau, M. (2011) in Procaryotic Antimicrobial Peptides: from Genes to Applications (Drider, D., and Rebuffat, S., eds) pp. 255-288, Springer Science Media, New York
10. Krone, W. J., de Vries, P., Koningstein, G., de Jonge, A. J., de Graaf, F. K., and Oudega, B. (1986) J. Bacteriol. 166, 260-268
11. Housden, N. G., Loftus, S. R., Moore, G. R., James, R., and Kleanthous, C. (2005) Proc. Natl. Acad. Sci. U.S.A. 102, 13849-13854
12. Duché, D., Frenkian, A., Prima, V., and Lloubès, R. (2006) J. Bacteriol. 188, 8593-8600
13. Zhang, Y., Vankemmelbeke, M. N., Holland, L. E., Walker, D. C., James, R., and Penfold, C. N. (2008) J. Bacteriol. 190, 4342-4350
14. Mosbahi, K., Lemaître, C., Keeble, A. H., Mobasheri, H., Morel, B., James, R., Moore, G. R., Lea, E. J., and Kleanthous, C. (2002) Nat. Struct. Biol. 9, 476-484
15. Mosbahi, K., Walker, D., Lea, E., Moore, G. R., James, R., and Kleanthous, C. (2004) J. Biol. Chem. 279, 22145-22151
16. Mosbahi, K., Walker, D., James, R., Moore, G. R., and Kleanthous, C. (2006) Protein Sci. 15, 620-627
17. de Zamaroczy, M., Mora, L., Lecuyer, A., Géli, V., and Buckingham, R. H. (2001) Mol. Cell 8, 159-168
18. Liao, C. C., Hsiao, K. C., Liu, Y. W., Leng, P. H., Yuen, H. S., and Chak, K. F. (2001) Biochem. Biophys. Res. Commun. 284, 556-562
19. Shi, Z., Chak, K. F., and Yuan, H. S. (2005) J. Biol. Chem. 280, 24663-24668
20. de Zamaroczy, M., and Buckingham, R. H. (2002) Biochimie 84, 423-432
21. Sharma, O., Yamashita, E., Zhalnina, M. V., Zakharov, S. D., Datsenko, K. A., Wanner, B. L., and Cramer, W. A. (2007) J. Biol. Chem. 282, 23163-23170
22. Kramer, R. A., Vandeputte-Rutten, L., de Roon, G. J., Gros, P., Dekker, N., and Egmond, M. R. (2001) FEBS Lett. 505, 426-430
23. Stumpe, S., Schmid, R., Stephens, D. L., Georgiou, G., and Bakker, E. P. (1998) J. Bacteriol. 180, 4002-4006
24. Masi, M., Vuong, P., Humbard, M., Malone, K., and Misra, R. (2007) J. Bacteriol. 189, 2667-2676
25. Duché, D., Issouf, M., and Lloubès, R. (2009) J. Biochem. 145, 95-101
26. Walker, D., Mosbahi, K., Vankemmelbeke, M., James, R., and Kleanthous, C. (2007) J. Biol. Chem. 282, 31389-31397
27. Graille, M., Mora, L., Buckingham, R. H., van Tilbeurgh, H., and de Zamaroczy, M. (2004) EMBO J. 23, 1474-1482
28. Paetzel, M., Strynadka, N. C., Tschantz, W. R., Casareno, R., Bullinger, P. R., and Dalbey, R. E. (1997) J. Biol. Chem. 272, 9994-10003
29. Wu, Y., Li, Q., and Chen, X. Z. (2007) Nat. Protoc. 2, 3278-3284
30. Betton, J. M., and Hofnung, M. (1996) J. Biol. Chem. 271, 8046-8052
31. Kramer, R. A., Zandwijken, D., Egmond, M. R., and Dekker, N. (2000) Eur. J. Biochem. 267, 885-893
32. Kramer, R. A., Brandenburg, K., Vandeputte-Rutten, L., Werkhoven, M., Gros, P., Dekker, N., and Egmond, M. R. (2002) Eur. J. Biochem. 269, 1746-1752
33. Dalbey, R. E., Lively, M. O., Bron, S., and van Dijl, J. M. (1997) Protein Sci. 6, 1129-1138
34. Sugimura, K., and Nishihara, T. (1988) J. Bacteriol. 170, 5625-5632
35. Tschantz, W. R., Sung, M., Delgado-Partin, V. M., and Dalbey, R. E. (1993) J. Biol. Chem. 268, 27349-27354
36. Kramer, R. A., Dekker, N., and Egmond, M. R. (2000) FEBS Lett. 468, 220-224
37. Grodberg, J., Lundrigan, M. D., Toledo, D. L., Mangel, W. F., and Dunn, J. J. (1988) Nucleic Acids Res. 16, 1209
38. Soelaiman, S., Jakes, K., Wu, N., Li, C., and Shoham, M. (2001) Mol. Cell 8, 1053-1062
39. Higgs, P. I., Larsen, R. A., and Postle, K. (2002) Mol. Microbiol. 44, 271-281
40. Mora, L., Diaz, N., Buckingham, R. H., and de Zamaroczy, M. (2005) J. Bacteriol. 187, 2693-2697
41. Kurisu, G., Zakharov, S. D., Zhalnina, M. V., Bano, S., Eroukova, V. Y., Rokitskaya, T. I., Antonenko, Y. N., Wiener, M. C., and Cramer, W. A. (2003) Nat. Struct. Biol. 10, 948-954
42. Sharma, O., and Cramer, W. A. (2007) J. Bacteriol. 189, 363-368
43. Ito, K., and Akiyama, Y. (2005) Annu. Rev. Microbiol. 59, 211-231
44. Bieniossek, C., Niederhauser, B., and Baumann, U. M. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 21579-21584
45. Striebel, F., Kress, W., and Weber-Ban, E. (2009) Curr. Opin. Struct. Biol. 19, 209-217
46. Herman, C., Prakash, S., Lu, C. Z., Matouschek, A., and Gross, C. A. (2003) Mol. Cell 11, 659-669
47. Ayuso-Tejedor, S., Nishikori, S., Okuno, T., Ogura, T., and Sancho, J. (2010) J. Struct. Biol. 171, 117-124
48. Narberhaus, F., Obrist, M., Führer, F., and Langklotz, S. (2009) Res. Microbiol. 160, 652-659
49. Suno, R., Niwa, H., Tsuchiya, D., Zhang, X., Yoshida, M., and Morikawa, K. (2006) Mol. Cell 22, 575-585
50. Okuno, T., Yamanaka, K., and Ogura, T. (2006) Genes Cells 11, 261-268
51. Akiyama, Y. (2009) J. Biochem. 146, 449-454
52. Tsai, B., Rodighiero, C., Lencer, W. I., and Rapoport, T. A. (2001) Cell 104, 937-948
53. Lencer, W. I., and Tsai, B. (2003) Trends Biochem. Sci. 28, 639-645
54. Vandeputte-Rutten, L., Kramer, R. A., Kroon, J., Dekker, N., Egmond, M. R., and Gros, P. (2001) EMBO J. 20, 5033-5039
55. Kleanthous, C. (2010) Nat. Rev. Microbiol. 8, 843-848
56. Vankemmelbeke, M., Zhang, Y., Moore, G. R., Kleanthous, C., Penfold, C. N., and James, R. (2009) J. Biol. Chem. 284, 18932-18941
57. Hilsenbeck, J. L., Park, H., Chen, G., Youn, B., Postle, K., and Kang, C. (2004) Mol. Microbiol. 51, 711-720
58. Paetzel, M., Dalbey, R. E., and Strynadka, N. C. (1998) Nature 396, 186-190
59. Akiyama, Y., and Ito, K. (1990) Biochem. Biophys. Res. Commun. 167, 711-715
60. Studier, F. W., and Moffatt, B. A. (1986) J. Mol. Biol. 189, 113-130
61. Elish, M. E., Pierce, J. R., and Earhart, C. F. (1988) J. Gen. Microbiol. 134, 1355-1364
62. Paquelin, A., Ghigo, J. M., Bertin, S., and Wandersman, C. (2001) Mol. Microbiol. 42, 995-1005
63. Dubuisson, J. F., Vianney, A., Hugouvieux-Cotte-Pattat, N., and Lazzaroni, J. C. (2005) Microbiology 151, 3337-3347
64. Tatsuta, T., Tomoyasu, T., Bukau, B., Kitagawa, M., Mori, H., Karata, K., and Ogura, T. (1998) Mol. Microbiol. 30, 583-593
65. Dalbey, R. E., and Wickner, W. (1985) J. Biol. Chem. 260, 15925-15931
66. Grodberg, J., and Dunn, J. J. (1988) J. Bacteriol. 170, 1245-1253
67. Akiyama, Y., Yoshihisa, T., and Ito, K. (1995) J. Biol. Chem. 270, 23485-23490
68. Frey, J., Ghersa, P., Palacios, P. G., and Belet, M. (1986) J. Bacteriol. 166, 15-19
69. Masaki, H., and Ohta, T. (1985) J. Mol. Biol. 182, 217-227
70. van Roosmalen, M. L., Jongbloed, J. D., de Jonf, A., van Eerden, J., Venema, G., Bron, S., and van Dijl, J. M. (2001) Microbiology 147, 909-917
71. Qiagen (2003) The QIAexpressionist: A Handbook for High-level Expression and Purification of 6xHis-tagged Proteins, 4th Ed., Hilden, Germany