메뉴 건너뛰기




Volumn 185, Issue 20, 2003, Pages 6051-6056

A second PDZ-containing serine protease contributes to activation of the sporulation transcription factor σK in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN CTPB; PROTEIN SPOIVB; SERINE PROTEINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0141925896     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.20.6051-6056.2003     Document Type: Article
Times cited : (29)

References (42)
  • 1
    • 0033568606 scopus 로고    scopus 로고
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor. Genes Dev. 13:2449-2461.
    • (1999) Genes Dev. , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 3
    • 0034696581 scopus 로고    scopus 로고
    • Substrate recognition through a PDZ domain in tail-specific protease
    • Beebe, K. D., J. Shin, J. Peng, C. Chaudhury, J. Khera, and D. Pei. 2000. Substrate recognition through a PDZ domain in tail-specific protease. Biochemistry 39:3149-3155.
    • (2000) Biochemistry , vol.39 , pp. 3149-3155
    • Beebe, K.D.1    Shin, J.2    Peng, J.3    Chaudhury, C.4    Khera, J.5    Pei, D.6
  • 5
    • 0025303604 scopus 로고
    • A forespore checkpoint for mother cell gene expression during development in B. subtilis
    • Cutting, S., V. Oke, A. Driks, R. Losick, S. Lu, and L. Kroos. 1990. A forespore checkpoint for mother cell gene expression during development in B. subtilis. Cell 62:239-250.
    • (1990) Cell , vol.62 , pp. 239-250
    • Cutting, S.1    Oke, V.2    Driks, A.3    Losick, R.4    Lu, S.5    Kroos, L.6
  • 6
    • 0026066575 scopus 로고
    • Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis
    • Cutting, S., S. Roels, and R. Losick. 1991. Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis. J. Mol. Biol. 221:1237-1256.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1237-1256
    • Cutting, S.1    Roels, S.2    Losick, R.3
  • 9
    • 0029097383 scopus 로고
    • K processing during spore formation in Bacillus subtilis
    • K processing during spore formation in Bacillus subtilis. J. Bacteriol. 177:4825-4827.
    • (1995) J. Bacteriol. , vol.177 , pp. 4825-4827
    • Gomez, M.1    Cutting, S.2    Stragier, P.3
  • 11
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guerout-Fleury, A. M., K. Shazand, N. Frandsen, and P. Stragier. 1995. Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167:335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guerout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 13
    • 0036135494 scopus 로고    scopus 로고
    • The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases
    • Hoa, N. T., J. A. Brannigan, and S. M. Cutting. 2002. The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases. J. Bacteriol. 184:191-199.
    • (2002) J. Bacteriol. , vol.184 , pp. 191-199
    • Hoa, N.T.1    Brannigan, J.A.2    Cutting, S.M.3
  • 14
    • 0034973190 scopus 로고    scopus 로고
    • The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions
    • Hoa, N. T., J. A. Brannigan, and S. M. Cutting. 2001. The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions. J. Bacteriol. 183:4364-4373.
    • (2001) J. Bacteriol. , vol.183 , pp. 4364-4373
    • Hoa, N.T.1    Brannigan, J.A.2    Cutting, S.M.3
  • 15
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • Hung, A. Y., and M. Sheng. 2002. PDZ domains: structural modules for protein complex assembly. J. Biol. Chem. 277:5699-5702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 16
    • 0037102458 scopus 로고    scopus 로고
    • E pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA
    • E pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA. Genes Dev. 16:2147-2155.
    • (2002) Genes Dev. , vol.16 , pp. 2147-2155
    • Kanehara, K.1    Ito, K.2    Akiyama, Y.3
  • 17
    • 0028841887 scopus 로고
    • Identification of active site residues of the Tsp protease
    • Keiler, K. C., and R. T. Sauer. 1995. Identification of active site residues of the Tsp protease. J. Biol. Chem. 270:28864-28868.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28864-28868
    • Keiler, K.C.1    Sauer, R.T.2
  • 18
    • 0024575242 scopus 로고
    • Switch protein alters specificity of RNA polymerase containing a compartment-specific sigma factor
    • Kroos, L., B. Kunkel, and R. Losick. 1989. Switch protein alters specificity of RNA polymerase containing a compartment-specific sigma factor. Science 243:526-529.
    • (1989) Science , vol.243 , pp. 526-529
    • Kroos, L.1    Kunkel, B.2    Losick, R.3
  • 19
    • 0033659766 scopus 로고    scopus 로고
    • Regulation of sigma factor activity during Bacillus subtilis development
    • Kroos, L., and Y. T. Yu. 2000. Regulation of sigma factor activity during Bacillus subtilis development. Curr. Opin. Microbiol. 3:553-560.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 553-560
    • Kroos, L.1    Yu, Y.T.2
  • 20
    • 0036777451 scopus 로고    scopus 로고
    • K processing during Bacillus subtilis sporulation despite the loss of SpoIVFA upon translational arrest
    • K processing during Bacillus subtilis sporulation despite the loss of SpoIVFA upon translational arrest. J. Bacteriol. 184:5393-5401.
    • (2002) J. Bacteriol. , vol.184 , pp. 5393-5401
    • Kroos, L.1    Yu, Y.T.2    Mills, D.3    Ferguson-Miller, S.4
  • 21
    • 0033823061 scopus 로고    scopus 로고
    • Crystal structures of the photosystem II D1 C-terminal processing protease
    • Liao, D. I., J. Qian, D. A. Chisholm, D. B. Jordan, and B. A. Diner. 2000. Crystal structures of the photosystem II D1 C-terminal processing protease. Nat. Struct. Biol. 7:749-753.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 749-753
    • Liao, D.I.1    Qian, J.2    Chisholm, D.A.3    Jordan, D.B.4    Diner, B.A.5
  • 22
    • 0028835710 scopus 로고
    • K in the absence of other sporulation gene products
    • K in the absence of other sporulation gene products. J. Bacteriol. 177:1082-1085.
    • (1995) J. Bacteriol. , vol.177 , pp. 1082-1085
    • Lu, S.1    Cutting, S.2    Kroos, L.3
  • 23
    • 0030457816 scopus 로고    scopus 로고
    • A new Bacillus subtilis gene with homology to Escherichia coli prc
    • Marasco, R., M. Varcamonti, E. Ricca, and M. Sacco. 1996. A new Bacillus subtilis gene with homology to Escherichia coli prc. Gene 183:149-152.
    • (1996) Gene , vol.183 , pp. 149-152
    • Marasco, R.1    Varcamonti, M.2    Ricca, E.3    Sacco, M.4
  • 25
    • 0029786970 scopus 로고    scopus 로고
    • Molecular studies of CtpA, the carboxyl-terminal processing protease for the D1 protein of the photosystem II reaction center in higher plants
    • Oelmuller, R., R. G. Herrmann, and H. B. Pakrasi. 1996. Molecular studies of CtpA, the carboxyl-terminal processing protease for the D1 protein of the photosystem II reaction center in higher plants. J. Biol. Chem. 271:21848-21852.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21848-21852
    • Oelmuller, R.1    Herrmann, R.G.2    Pakrasi, H.B.3
  • 26
    • 0034764908 scopus 로고    scopus 로고
    • Self-reinforcing activation of a cell-specific transcription factor by proteolysis of an anti-sigma factor in B. subtilis
    • Pan, Q., D. A. Garsin, and R. Losick. 2001. Self-reinforcing activation of a cell-specific transcription factor by proteolysis of an anti-sigma factor in B. subtilis. Mol. Cell 8:873-883.
    • (2001) Mol. Cell , vol.8 , pp. 873-883
    • Pan, Q.1    Garsin, D.A.2    Losick, R.3
  • 27
    • 0002305548 scopus 로고    scopus 로고
    • Sporulation genes and intercompartmental regulation
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.). American Society for Microbiology, Washington, D.C.
    • Piggot, P. J., and R. Losick. 2002. Sporulation genes and intercompartmental regulation, p. 483-518. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and its closest relatives: from genes to cells. American Society for Microbiology, Washington, D.C.
    • (2002) Bacillus Subtilis and Its Closest Relatives: From Genes to Cells , pp. 483-518
    • Piggot, P.J.1    Losick, R.2
  • 29
    • 0030155665 scopus 로고    scopus 로고
    • Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis
    • Resnekov, O., S. Alper, and R. Losick. 1996. Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis. Genes Cells 1:529-542.
    • (1996) Genes Cells , vol.1 , pp. 529-542
    • Resnekov, O.1    Alper, S.2    Losick, R.3
  • 30
    • 0032539926 scopus 로고    scopus 로고
    • Negative regulation of the proteolytic activation of a developmental transcription factor in Bacillus subtilis
    • Resnekov, O., and R. Losick. 1998. Negative regulation of the proteolytic activation of a developmental transcription factor in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 95:3162-3167.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3162-3167
    • Resnekov, O.1    Losick, R.2
  • 31
    • 0026724088 scopus 로고
    • K processing during sporulation in Bacillus subtilis
    • K processing during sporulation in Bacillus subtilis. J. Bacteriol. 174:3177-3184.
    • (1992) J. Bacteriol. , vol.174 , pp. 3177-3184
    • Ricca, E.1    Cutting, S.2    Losick, R.3
  • 32
    • 0033593022 scopus 로고    scopus 로고
    • A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors
    • Rudner, D. Z., P. Fawcett, and R. Losick. 1999. A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors. Proc. Natl. Acad. Sci. USA 96:14765-14770.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14765-14770
    • Rudner, D.Z.1    Fawcett, P.2    Losick, R.3
  • 33
    • 0037089590 scopus 로고    scopus 로고
    • K processing enzyme to its inhibitor and dictates its subcellular localization
    • K processing enzyme to its inhibitor and dictates its subcellular localization. Genes Dev. 16:1007-1018.
    • (2002) Genes Dev. , vol.16 , pp. 1007-1018
    • Rudner, D.Z.1    Losick, R.2
  • 34
    • 0037172980 scopus 로고    scopus 로고
    • Evidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture
    • Rudner, D. Z., Q. Pan, and R. M. Losick. 2002. Evidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture. Proc. Natl. Acad. Sci. USA 99:8701-8706.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8701-8706
    • Rudner, D.Z.1    Pan, Q.2    Losick, R.M.3
  • 35
    • 0028064901 scopus 로고
    • Molecular cloning and characterization of the ctpA gene encoding a carboxyl-terminal processing protease. Analysis of a spontaneous photosystem II-deficient mutant strain of the cyanobacterium Synechocystis sp. PCC 6803
    • Shestakov, S. V., P. R. Anbudurai, G. E. Stanbekova, A. Gadzhiev, L. K. Lind, and H. B. Pakrasi. 1994. Molecular cloning and characterization of the ctpA gene encoding a carboxyl-terminal processing protease. Analysis of a spontaneous photosystem II-deficient mutant strain of the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 269:19354-19359.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19354-19359
    • Shestakov, S.V.1    Anbudurai, P.R.2    Stanbekova, G.E.3    Gadzhiev, A.4    Lind, L.K.5    Pakrasi, H.B.6
  • 36
    • 0026513218 scopus 로고
    • Tsp: A tail-specific protease that selectively degrades proteins with nonpolar C termini
    • Silber, K. R., K. C. Keiler, and R. T. Sauer. 1992. Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini. Proc. Natl. Acad. Sci. USA 89:295-299.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 295-299
    • Silber, K.R.1    Keiler, K.C.2    Sauer, R.T.3
  • 39
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • Walsh, N. P., B. M. Alba, B. Bose, C. A. Gross, and R. T. Sauer. 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.
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 40
    • 0037418896 scopus 로고    scopus 로고
    • A stress sensor for the bacterial periplasm
    • Young, J. C., and F. U. Hartl. 2003. A stress sensor for the bacterial periplasm. Cell 113:1-2.
    • (2003) Cell , vol.113 , pp. 1-2
    • Young, J.C.1    Hartl, F.U.2
  • 41
    • 0020511586 scopus 로고
    • Genetic transposition and insertional mutagenesis in Bacillus subtilis with Streptococcus faecalis transposon Tn917
    • Youngman, P. J., J. B. Perkins, and R. Losick. 1983. Genetic transposition and insertional mutagenesis in Bacillus subtilis with Streptococcus faecalis transposon Tn917. Proc. Natl. Acad. Sci. USA 80:2305-2309.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2305-2309
    • Youngman, P.J.1    Perkins, J.B.2    Losick, R.3
  • 42
    • 0034035286 scopus 로고    scopus 로고
    • Evidence that SpoIVFB is a novel type of membrane metalloprotease governing intercompartmental communication during Bacillus subtilis sporulation
    • Yu, Y. T., and L. Kroos. 2000. Evidence that SpoIVFB is a novel type of membrane metalloprotease governing intercompartmental communication during Bacillus subtilis sporulation. J. Bacteriol. 182:3305-3309.
    • (2000) J. Bacteriol. , vol.182 , pp. 3305-3309
    • Yu, Y.T.1    Kroos, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.