YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA

EMBO Journal

Volumn 22, Issue 23, 2003, Pages 6389-6398

  Kanehara, Kazue ^a   Ito, Koreaki ^a   Akiyama, Yoshinori ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Extracytoplasmic stress response; Glutamine rich regions; PDZ domain; Regulated intramembrane proteolysis; Site 2 protease

Indexed keywords

BACTERIAL PROTEIN; GLUTAMINE; PDZ PROTEIN; PROTEIN RSEA; PROTEIN YAEL; SIGMA FACTOR; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; CONTROLLED STUDY; CYTOPLASM; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; STRESS;

AMINO ACID SEQUENCE; BINDING SITES; ENDOPEPTIDASES; ESCHERICHIA COLI PROTEINS; GENETIC COMPLEMENTATION TEST; GLUTAMINE; KINETICS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PLASMIDS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0346243935     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg602     Document Type: Article

References (31)

1. E-dependent extracytoplasmic response is controlled by the regulated proteolysis of an anti-σ factor. Genes Dev., 13, 2449-2461.
2. E activity. Mol. Microbiol., 406, 1323-1333.
3. E-dependent extracytoplasmic stress response. Genes Dev., 16, 2156-2168.
4. Brown, M.S., Ye, J., Rawson, R.B. and Goldstein, J.L. (2000) Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell, 100, 391-398.
5. E with the cytoplasmic domain of its anti-sigma RseA. Mol. Cell, 11, 1067-1078.
6. E-RNA polymerase. J. Biol. Chem., 275, 33898-33904.
7. Davis, R.W., Botstein, D. and Roth, J.R. (1980) Advanced Bacterial Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
8. E. Mol. Microbiol., 24, 373-385.
9. Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M. and MacKinnon, R. (1996) Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell, 85, 1067-1076.
10. Duncan, E.A., Dave, U.P., Sakai, J., Goldstein, J.L. and Brown, M.S. (1998) Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning. J. Biol. Chem., 273, 17801-17809.
11. Flynn, J.M., Neher, S.B., Kim, Y.I., Sauer, R.T. and Baker, T.A. (2003) Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell, 11, 671-683.
12. Harris, B.Z. and Lim, W.A. (2001) Mechanism and role of PDZ domains in signaling complex assembly. J. Cell Sci., 114, 3219-3231.
13. Hillier, B.J., Christopherson, K.S., Prehoda, K.E., Bredt, D. S. and Lim, W.A. (1999) Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science, 284, 812-815.
14. Kanehara, K., Akiyama, Y. and Ito, K. (2001) Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli. Gene, 281, 71-79.
15. E, RseA. Genes Dev., 16, 2147-2155.
16. Li, W., Srinivasula, S.M., Chai, J., Li, P., Wu, J.W., Zhang, Z., Alnemri, E.S. and Shi, Y. (2002) Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. Nat. Struct. Biol., 9, 436-441.
17. Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
18. Missiakas, D. and Raina, S. (1998) The extracytoplasmic function sigma factors: role and regulation. Mol. Microbiol., 28, 1059-1066.
19. E (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol. Microbiol., 24, 355-371.
20. Perutz, M.F., Johnson, T., Suzuki, M. and Finch, J.T. (1994) Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl Acad. Sci. USA, 91, 5355-5358.
21. Prentki, P. and Krisch, H.M. (1984) In vitro insertional mutagenesis with a selectable DNA fragment. Gene, 29, 303-313.
22. E and Cpx regulatory pathways: overlapping but distinct envelope stress responses. Curr. Opin. Microbiol., 2, 159-165.
23. Raivio, T.L. and Silhavy, T.J. (2001) Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol., 55, 591-624.
24. Sakai, J., Rawson, R.B., Espenshade, P.J., Cheng, D., Seegmiller, A.C., Goldstein, J.L. and Brown, M.S. (1998) Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol. Cell, 2, 505-514.
25. Sawano, A. and Miyawaki, A. (2000) Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis. Nucleic Acids Res., 28, E78.
26. Shimoike, T., Taura, T., Kihara, A., Yoshihisa, T., Akiyama, Y., Cannon, K. and Ito, K. (1995) Product of a new gene, syd, functionally interacts with SecY when overproduced in Escherichia coli. J. Biol. Chem., 270, 5519-5526.
27. Taura, T., Baba, T., Akiyama, Y. and Ito, K. (1993) Determinants of the quantity of the stable SecY complex in the Escherichia coli cell. J. Bacteriol., 175, 7771-7775.
28. Waller, P.R. and Sauer, R.T. (1996) Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol., 178, 1146-1153.
29. Walsh, N.P., Alba, B.M., Bose, B., Gross, C.A. and Sauer, R.T. (2003) OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell. 113, 61-71.
30. Weihofen, A. and Martoglio, B. (2003) Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides. Trends Cell Biol., 13, 71-78.
31. Ye, J., Rawson, R.B., Komuro, R., Chen, X., Dave, U.P., Prywes, R., Brown, M.S. and Goldstein, J.L. (2000) ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell, 6, 1355-1364.