메뉴 건너뛰기




Volumn 1828, Issue 12, 2013, Pages 2873-2885

Biochemical and structural insights into intramembrane metalloprotease mechanisms

Author keywords

CBS domain; Intramembrane metalloprotease; PDZ domain; RseP; S2P; SpoIVFB

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; MEMBRANE ENZYME; METALLOPROTEINASE; PDZ PROTEIN; RSEP PROTEIN; S2P PROTEIN; SPOIVFB PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 84885153827     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.03.032     Document Type: Review
Times cited : (42)

References (107)
  • 2
    • 0032965585 scopus 로고    scopus 로고
    • A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties
    • A. Lewis, and P. Thomas A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties Protein Sci. 8 1999 439 442 (Pubitemid 29072446)
    • (1999) Protein Science , vol.8 , Issue.2 , pp. 439-442
    • Lewis, A.P.1    Thomas, P.J.2
  • 3
  • 4
    • 0034035286 scopus 로고    scopus 로고
    • Evidence that SpoIVFB is a novel type of membrane metalloprotease governing intercompartmental communication during Bacillus subtilis sporulation
    • DOI 10.1128/JB.182.11.3305-3309.2000
    • Y.-T.N. Yu, and L. Kroos Evidence that SpoIVFB is a novel type of membrane metalloprotease governing intercompartmental communication during Bacillus subtilis sporulation J. Bacteriol. 182 2000 3305 3309 (Pubitemid 30326954)
    • (2000) Journal of Bacteriology , vol.182 , Issue.11 , pp. 3305-3309
    • Yu, Y.-T.N.1    Kroos, L.2
  • 6
    • 0035960904 scopus 로고    scopus 로고
    • Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli
    • DOI 10.1016/S0378-1119(01)00823-X, PII S037811190100823X
    • K. Kanehara, Y. Akiyama, and K. Ito Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli Gene 281 2001 71 79 (Pubitemid 34031906)
    • (2001) Gene , vol.281 , Issue.1-2 , pp. 71-79
    • Kanehara, K.1    Akiyama, Y.2    Ito, K.3
  • 8
    • 29344444795 scopus 로고    scopus 로고
    • Site-2 protease regulated intramembrane proteolysis: Sequence homologs suggest an ancient signaling cascade
    • DOI 10.1110/ps.051766506
    • L.N. Kinch, K. Ginalski, and N.V. Grishin Site-2 protease regulated intramembrane proteolysis: sequence homologs suggest an ancient signaling cascade Protein Sci. 15 2006 84 93 (Pubitemid 43004236)
    • (2006) Protein Science , vol.15 , Issue.1 , pp. 84-93
    • Kinch, L.N.1    Ginalski, K.2    Grishin, N.V.3
  • 9
    • 84869104770 scopus 로고    scopus 로고
    • Identification and characterization of five intramembrane metalloproteases in Anabaena variabilis
    • K. Chen, L. Gu, X. Xiang, M. Lynch, and R. Zhou Identification and characterization of five intramembrane metalloproteases in Anabaena variabilis J. Bacteriol. 194 2012 6105 6115
    • (2012) J. Bacteriol. , vol.194 , pp. 6105-6115
    • Chen, K.1    Gu, L.2    Xiang, X.3    Lynch, M.4    Zhou, R.5
  • 10
    • 84885175357 scopus 로고    scopus 로고
    • Bioinformatics perspective on rhomboid intramembrane protease evolution and function
    • (in this issue)
    • L.N. Kinch, and N.V. Grishin Bioinformatics perspective on rhomboid intramembrane protease evolution and function BBA Biomembr. 1828 2013 2937 2943 (in this issue)
    • (2013) BBA Biomembr. , vol.1828 , pp. 2937-2943
    • Kinch, L.N.1    Grishin, N.V.2
  • 11
    • 0032871073 scopus 로고    scopus 로고
    • Identification and characterization of a determinant (eep) on the Enterococcus faecalis chromosome that is involved in production of the peptide sex pheromone cAD1
    • F.Y. An, M.C. Sulavik, and D.B. Clewell Identification and characterization of a determinant (eep) on the Enterococcus faecalis chromosome that is involved in production of the peptide sex pheromone cAD1 J. Bacteriol. 181 1999 5915 5921 (Pubitemid 29459900)
    • (1999) Journal of Bacteriology , vol.181 , Issue.19 , pp. 5915-5921
    • An, F.Y.1    Sulavik, M.C.2    Clewell, D.B.3
  • 12
    • 14544270275 scopus 로고    scopus 로고
    • A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant
    • DOI 10.1111/j.1365-2958.2004.04443.x
    • J.C. Chen, P.H. Viollier, and L. Shapiro A membrane metalloprotease participates in the sequential degradation of a Caulobacter polarity determinant Mol. Microbiol. 55 2005 1085 1103 (Pubitemid 40299179)
    • (2005) Molecular Microbiology , vol.55 , Issue.4 , pp. 1085-1103
    • Chen, J.C.1    Viollier, P.H.2    Shapiro, L.3
  • 13
    • 33749183115 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2006.05402.x
    • M. Bramkamp, L. Weston, R.A. Daniel, and J. Errington Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis Mol. Microbiol. 62 2006 580 591 (Pubitemid 44477243)
    • (2006) Molecular Microbiology , vol.62 , Issue.2 , pp. 580-591
    • Bramkamp, M.1    Weston, L.2    Daniel, R.A.3    Errington, J.4
  • 14
    • 33746411866 scopus 로고    scopus 로고
    • Site-2 proteases in prokaryotes: Regulated intramembrane proteolysis expands to microbial pathogenesis
    • DOI 10.1016/j.micinf.2006.02.021, PII S1286457906001444
    • H. Makinoshima, and M.S. Glickman Site-2 proteases in prokaryotes: regulated intramembrane proteolysis expands to microbial pathogenesis Microbes Infect. 8 2006 1882 1888 (Pubitemid 44128885)
    • (2006) Microbes and Infection , vol.8 , Issue.7 , pp. 1882-1888
    • Makinoshima, H.1    Glickman, M.S.2
  • 15
    • 67349117281 scopus 로고    scopus 로고
    • Making the cut: Central roles of intramembrane proteolysis in pathogenic microorganisms
    • S. Urban Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms Nat. Rev. Microbiol. 7 2009 411 423
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 411-423
    • Urban, S.1
  • 17
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • DOI 10.1016/S1097-2765(00)00133-7
    • J. Ye, R.B. Rawson, R. Komuro, X. Chen, U.P. Dave, R. Prywes, M.S. Brown, and J.L. Goldstein ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs Mol. Cell 6 2000 1355 1364 (Pubitemid 32045928)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5    Prywes, R.6    Brown, M.S.7    Goldstein, J.L.8
  • 18
    • 32044453080 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response
    • DOI 10.1016/j.cell.2005.11.040, PII S0092867406000043
    • K. Zhang, X. Shen, J. Wu, K. Sakaki, T. Saunders, D.T. Rutkowski, S.H. Back, and R.J. Kaufman Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response Cell 124 2006 587 599 (Pubitemid 43199443)
    • (2006) Cell , vol.124 , Issue.3 , pp. 587-599
    • Zhang, K.1    Shen, X.2    Wu, J.3    Sakaki, K.4    Saunders, T.5    Rutkowski, D.T.6    Back, S.H.7    Kaufman, R.J.8
  • 19
    • 63649088506 scopus 로고    scopus 로고
    • Structure and mechanism of intramembrane protease
    • Y. Ha Structure and mechanism of intramembrane protease Semin. Cell Dev. Biol. 20 2009 240 250
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 240-250
    • Ha, Y.1
  • 20
    • 49549106231 scopus 로고    scopus 로고
    • Core principles of intramembrane proteolysis: Comparison of rhomboid and site-2 family proteases
    • S. Urban, and Y. Shi Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases Curr. Opin. Struct. Biol. 18 2008 432 441
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 432-441
    • Urban, S.1    Shi, Y.2
  • 21
    • 65249188697 scopus 로고    scopus 로고
    • Intramembrane proteolysis
    • M.S. Wolfe Intramembrane proteolysis Chem. Rev. 109 2009 1599 1612
    • (2009) Chem. Rev. , vol.109 , pp. 1599-1612
    • Wolfe, M.S.1
  • 22
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • DOI 10.1126/science.1150755
    • L. Feng, H. Yan, Z. Wu, N. Yan, Z. Wang, P.D. Jeffrey, and Y. Shi Structure of a site-2 protease family intramembrane metalloprotease Science 318 2007 1608 1612 (Pubitemid 350233656)
    • (2007) Science , vol.318 , Issue.5856 , pp. 1608-1612
    • Feng, L.1    Yan, H.2    Wu, Z.3    Yan, N.4    Wang, Z.5    Jeffrey, P.D.6    Shi, Y.7
  • 23
    • 0043172415 scopus 로고    scopus 로고
    • The SREBP pathway - Insights from insigs and insects
    • DOI 10.1038/nrm1174
    • R.B. Rawson The SREBP pathway - insights from Insigs and insects Nat. Rev. Mol. Cell Biol. 4 2003 631 640 (Pubitemid 36934965)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.8 , pp. 631-640
    • Rawson, R.B.1
  • 24
    • 0033618342 scopus 로고    scopus 로고
    • Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins
    • N. Zelenski, R. Rawson, M. Brown, and J. Goldstein Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins J. Biol. Chem. 274 1999 21973 21980
    • (1999) J. Biol. Chem. , vol.274 , pp. 21973-21980
    • Zelenski, N.1    Rawson, R.2    Brown, M.3    Goldstein, J.4
  • 25
    • 0030155665 scopus 로고    scopus 로고
    • Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis
    • O. Resnekov, S. Alper, and R. Losick Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilis Genes Cells 1 1996 529 542 (Pubitemid 126673147)
    • (1996) Genes to Cells , vol.1 , Issue.6 , pp. 529-542
    • Resnekov, O.1    Alper, S.2    Losick, R.3
  • 26
    • 0037089590 scopus 로고    scopus 로고
    • K processing enzyme to its inhibitor and dictates its subcellular localization
    • DOI 10.1101/gad.977702
    • K processing enzyme to its inhibitor and dictates its subcellular localization Genes Dev. 16 2002 1007 1018 (Pubitemid 34408549)
    • (2002) Genes and Development , vol.16 , Issue.8 , pp. 1007-1018
    • Rudner, D.Z.1    Losick, R.2
  • 28
    • 26244460528 scopus 로고    scopus 로고
    • K activity
    • DOI 10.1111/j.1365-2958.2005.04811.x
    • X. Jiang, A. Rubio, S. Chiba, and K. Pogliano Engulfment-regulated proteolysis of SpoIIQ: evidence that dual checkpoints control sigma activity Mol. Microbiol. 58 2005 102 115 (Pubitemid 41415034)
    • (2005) Molecular Microbiology , vol.58 , Issue.1 , pp. 102-115
    • Jiang, X.1    Rubio, A.2    Chiba, S.3    Pogliano, K.4
  • 29
    • 0031596513 scopus 로고    scopus 로고
    • The prosequence of pro-σ(K) promotes membrane association and inhibits RNA polymerase core binding
    • K promotes membrane association and inhibits RNA polymerase core binding J. Bacteriol. 180 1998 2434 2441 (Pubitemid 28217358)
    • (1998) Journal of Bacteriology , vol.180 , Issue.9 , pp. 2434-2441
    • Zhang, B.1    Hofmeister, A.2    Kroos, L.3
  • 30
    • 0026066575 scopus 로고
    • Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis
    • S. Cutting, S. Roels, and R. Losick Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis J. Mol. Biol. 221 1991 1237 1256 (Pubitemid 121003451)
    • (1991) Journal of Molecular Biology , vol.221 , Issue.4 , pp. 1237-1256
    • Cutting, S.1    Roels, S.2    Losick, R.3
  • 31
    • 0033988056 scopus 로고    scopus 로고
    • Membrane topology of the Bacillus subtilis pro-σ(K) processing complex
    • DOI 10.1128/JB.182.2.278-285.2000
    • K processing complex J. Bacteriol. 182 2000 278 285 (Pubitemid 30030109)
    • (2000) Journal of Bacteriology , vol.182 , Issue.2 , pp. 278-285
    • Green, D.H.1    Cutting, S.M.2
  • 32
    • 70349488828 scopus 로고    scopus 로고
    • Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP
    • R. Zhou, C. Cusumano, D. Sui, R.M. Garavito, and L. Kroos Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP Proc. Natl. Acad. Sci. U. S. A. 106 2009 16174 16179
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16174-16179
    • Zhou, R.1    Cusumano, C.2    Sui, D.3    Garavito, R.M.4    Kroos, L.5
  • 33
    • 0033568606 scopus 로고    scopus 로고
    • The Escherichia coli σ(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-σ factor
    • DOI 10.1101/gad.13.18.2449
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor Genes Dev. 13 1999 2449 2461 (Pubitemid 29453615)
    • (1999) Genes and Development , vol.13 , Issue.18 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 34
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
    • DOI 10.1016/S0092-8674(04)00454-4, PII S0092867404004544
    • C. Wilken, K. Kitzing, R. Kurzbauer, M. Ehrmann, and T. Clausen Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease Cell 117 2004 483 494 (Pubitemid 38610233)
    • (2004) Cell , vol.117 , Issue.4 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5
  • 36
    • 0346243935 scopus 로고    scopus 로고
    • YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA
    • DOI 10.1093/emboj/cdg602
    • K. Kanehara, K. Ito, and Y. Akiyama YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA EMBO J. 22 2003 6389 6398 (Pubitemid 37522595)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6389-6398
    • Kanehara, K.1    Ito, K.2    Akiyama, Y.3
  • 37
    • 1942468856 scopus 로고    scopus 로고
    • Dispensable PDZ domain of Escherichia coli YaeL essential protease
    • DOI 10.1111/j.1365-2958.2004.03985.x
    • C. Bohn, J. Collier, and P. Bouloc Dispensable PDZ domain of Escherichia coli YaeL essential protease Mol. Microbiol. 52 2004 427 435 (Pubitemid 38520713)
    • (2004) Molecular Microbiology , vol.52 , Issue.2 , pp. 427-435
    • Bohn, C.1    Collier, J.2    Bouloc, P.3
  • 39
    • 58049199407 scopus 로고    scopus 로고
    • A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli
    • K. Inaba, M. Suzuki, K. Maegawa, S. Akiyama, K. Ito, and Y. Akiyama A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli J. Biol. Chem. 283 2008 35042 35052
    • (2008) J. Biol. Chem. , vol.283 , pp. 35042-35052
    • Inaba, K.1    Suzuki, M.2    Maegawa, K.3    Akiyama, S.4    Ito, K.5    Akiyama, Y.6
  • 40
    • 70349299921 scopus 로고    scopus 로고
    • Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage
    • X. Li, B. Wang, L. Feng, H. Kang, Y. Qi, J. Wang, and Y. Shi Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage Proc. Natl. Acad. Sci. U. S. A. 106 2009 14837 14842
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14837-14842
    • Li, X.1    Wang, B.2    Feng, L.3    Kang, H.4    Qi, Y.5    Wang, J.6    Shi, Y.7
  • 41
    • 0030604717 scopus 로고    scopus 로고
    • Sterol-regulated release of SREBP-2 from cell membrane requires two sequential cleavages, one within a transmembrane domain
    • J. Sakai, E.A. Duncan, R.B. Rawson, X. Hua, M.S. Brown, and J.L. Goldstein Sterol-regulated release of SREBP-2 from cell membrane requires two sequential cleavages, one within a transmembrane domain Cell 85 1996 1037 1048
    • (1996) Cell , vol.85 , pp. 1037-1048
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3    Hua, X.4    Brown, M.S.5    Goldstein, J.L.6
  • 42
    • 0030854859 scopus 로고    scopus 로고
    • Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPS) and SREBP cleavage-activating protein
    • DOI 10.1074/jbc.272.32.20213
    • J. Sakai, A. Nohturfft, D. Cheng, Y.K. Ho, M.S. Brown, and J.L. Goldstein Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein J. Biol. Chem. 272 1997 20213 20221 (Pubitemid 27340132)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.32 , pp. 20213-20221
    • Sakai, J.1    Nohturfft, A.2    Cheng, D.3    Ho, Y.K.4    Brown, M.S.5    Goldstein, J.L.6
  • 44
    • 0025303604 scopus 로고
    • A forespore checkpoint for mother-cell gene expression during development in Bacillus subtilis
    • S. Cutting, V. Oke, A. Driks, R. Losick, S. Lu, and L. Kroos A forespore checkpoint for mother-cell gene expression during development in Bacillus subtilis Cell 62 1990 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
  • 47
    • 33745512838 scopus 로고    scopus 로고
    • A Branched Pathway Governing the Activation of a Developmental Transcription Factor by Regulated Intramembrane Proteolysis
    • DOI 10.1016/j.molcel.2006.05.019, PII S1097276506003340
    • N. Campo, and D.Z. Rudner A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis Mol. Cell 23 2006 25 35 (Pubitemid 43963443)
    • (2006) Molecular Cell , vol.23 , Issue.1 , pp. 25-35
    • Campo, N.1    Rudner, D.Z.2
  • 48
    • 0141677809 scopus 로고    scopus 로고
    • K in Bacillus subtilis
    • DOI 10.1046/j.1365-2958.2003.03651.x
    • K in Bacillus subtilis Mol. Microbiol. 49 2003 1425 1434 (Pubitemid 37153507)
    • (2003) Molecular Microbiology , vol.49 , Issue.5 , pp. 1425-1434
    • Dong, T.C.1    Cutting, S.M.2
  • 49
    • 27444444314 scopus 로고    scopus 로고
    • K during Bacillus subtilis development
    • DOI 10.1111/j.1365-2958.2005.04870.x
    • K during Bacillus subtilis development Mol. Microbiol. 58 2005 835 846 (Pubitemid 41532479)
    • (2005) Molecular Microbiology , vol.58 , Issue.3 , pp. 835-846
    • Zhou, R.1    Kroos, L.2
  • 50
    • 34547804226 scopus 로고    scopus 로고
    • K in Bacillus subtilis
    • DOI 10.1128/JB.00399-07
    • N. Campo, and D.Z. Rudner SpoIVB and CtpB are both forespore signals in the activation of the sporulation transcription factor sigmaK in Bacillus subtilis J. Bacteriol. 189 2007 6021 6027 (Pubitemid 47236154)
    • (2007) Journal of Bacteriology , vol.189 , Issue.16 , pp. 6021-6027
    • Campo, N.1    Rudner, D.Z.2
  • 52
    • 14744274820 scopus 로고    scopus 로고
    • Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum
    • DOI 10.1111/j.1365-2958.2005.04501.x
    • T. Doan, K.A. Marquis, and D.Z. Rudner Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum Mol. Microbiol. 55 2005 1767 1781 (Pubitemid 40445212)
    • (2005) Molecular Microbiology , vol.55 , Issue.6 , pp. 1767-1781
    • Doan, T.1    Marquis, K.A.2    Rudner, D.Z.3
  • 53
    • 0037115463 scopus 로고    scopus 로고
    • A cytoskeleton-like role for the bacterial cell wall during engulfment of the Bacillus subtilis forespore
    • DOI 10.1101/gad.1039902
    • A. Abanes-De Mello, Y.L. Sun, S. Aung, and K. Pogliano A cytoskeleton-like role for the bacterial cell wall during engulfment of the Bacillus subtilis forespore Genes Dev. 16 2002 3253 3264 (Pubitemid 36025977)
    • (2002) Genes and Development , vol.16 , Issue.24 , pp. 3253-3264
    • Abanes-De Mello, A.1    Sun, Y.-L.2    Aung, S.3    Pogliano, K.4
  • 55
    • 76749120537 scopus 로고    scopus 로고
    • A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis
    • C. Morlot, T. Uehara, K.A. Marquis, T.G. Bernhardt, and D.Z. Rudner A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis Genes Dev. 24 2010 411 422
    • (2010) Genes Dev. , vol.24 , pp. 411-422
    • Morlot, C.1    Uehara, T.2    Marquis, K.A.3    Bernhardt, T.G.4    Rudner, D.Z.5
  • 56
    • 10044268409 scopus 로고    scopus 로고
    • Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization
    • DOI 10.1101/gad.1252704
    • B. Blaylock, X. Jiang, A. Rubio, C.P. Moran Jr., and K. Pogliano Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization Genes Dev. 18 2004 2916 2928 (Pubitemid 39602310)
    • (2004) Genes and Development , vol.18 , Issue.23 , pp. 2916-2928
    • Blaylock, B.1    Jiang, X.2    Rubio, A.3    Moran Jr., C.P.4    Pogliano, K.5
  • 57
    • 33748201611 scopus 로고    scopus 로고
    • Forespore Engulfment Mediated by a Ratchet-Like Mechanism
    • DOI 10.1016/j.cell.2006.06.053, PII S0092867406010142
    • D.H. Broder, and K. Pogliano Forespore engulfment mediated by a ratchet-like mechanism Cell 126 2006 917 928 (Pubitemid 44310773)
    • (2006) Cell , vol.126 , Issue.5 , pp. 917-928
    • Broder, D.H.1    Pogliano, K.2
  • 58
    • 47249121296 scopus 로고    scopus 로고
    • A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels
    • DOI 10.1111/j.1365-2958.2008.06289.x
    • A.H. Camp, and R. Losick A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels Mol. Microbiol. 69 2008 402 417 (Pubitemid 351988013)
    • (2008) Molecular Microbiology , vol.69 , Issue.2 , pp. 402-417
    • Camp, A.H.1    Losick, R.2
  • 60
    • 65249114670 scopus 로고    scopus 로고
    • A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis
    • A.H. Camp, and R. Losick A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis Genes Dev. 23 2009 1014 1024
    • (2009) Genes Dev. , vol.23 , pp. 1014-1024
    • Camp, A.H.1    Losick, R.2
  • 61
    • 68249127846 scopus 로고    scopus 로고
    • Novel secretion apparatus maintains spore integrity and developmental gene expression in Bacillus subtilis
    • T. Doan, C. Morlot, J. Meisner, M. Serrano, A.O. Henriques, C.P. Moran Jr., and D.Z. Rudner Novel secretion apparatus maintains spore integrity and developmental gene expression in Bacillus subtilis PLoS Genet. 5 2009 e1000566
    • (2009) PLoS Genet. , vol.5 , pp. 1000566
    • Doan, T.1    Morlot, C.2    Meisner, J.3    Serrano, M.4    Henriques, A.O.5    Moran, Jr.C.P.6    Rudner, D.Z.7
  • 62
    • 34047247722 scopus 로고    scopus 로고
    • Impact of membrane fusion and proteolysis on SpoIIQ dynamics and interaction with SpoIIIAH
    • DOI 10.1074/jbc.M606056200
    • S. Chiba, K. Coleman, and K. Pogliano Impact of membrane fusion and proteolysis on SpoIIQ dynamics and interaction with SpoIIIAH J. Biol. Chem. 282 2007 2576 2586 (Pubitemid 47076751)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.4 , pp. 2576-2586
    • Chiba, S.1    Coleman, K.2    Pogliano, K.3
  • 63
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • DOI 10.1016/S0968-0004(96)30046-7, PII S0968000496300467
    • A. Bateman The structure of a domain common to archaebacteria and the homocystinuria disease protein Trends Biochem. Sci. 22 1997 12 13 (Pubitemid 27056090)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.1 , pp. 12-13
    • Bateman, A.1
  • 64
    • 27744463780 scopus 로고    scopus 로고
    • CBS domains: Structure, function, and pathology in human proteins
    • S. Ignoul, and J. Eggermont CBS domains: structure, function, and pathology in human proteins Am. J. Physiol. Cell Physiol. 289 2005 C1369 C1378
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Ignoul, S.1    Eggermont, J.2
  • 65
    • 81555228426 scopus 로고    scopus 로고
    • The CBS domain: A protein module with an emerging prominent role in regulation
    • A.A. Baykov, H.K. Tuominen, and R. Lahti The CBS domain: a protein module with an emerging prominent role in regulation ACS Chem. Biol. 6 2011 1156 1163
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1156-1163
    • Baykov, A.A.1    Tuominen, H.K.2    Lahti, R.3
  • 67
    • 56949096401 scopus 로고    scopus 로고
    • e envelope stress response
    • E envelope stress response Curr. Opin. Microbiol. 11 2008 535 540
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 535-540
    • Ades, S.E.1
  • 69
    • 58149287846 scopus 로고    scopus 로고
    • OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations
    • J. Sohn, and R.T. Sauer OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations Mol. Cell 33 2009 64 74
    • (2009) Mol. Cell , vol.33 , pp. 64-74
    • Sohn, J.1    Sauer, R.T.2
  • 70
    • 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
    • DOI 10.1016/S0092-8674(03)00203-4
    • N.P. Walsh, B.M. Alba, B. Bose, C.A. Gross, and R.T. Sauer OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain Cell 113 2003 61 71 (Pubitemid 36411960)
    • (2003) Cell , vol.113 , Issue.1 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 71
    • 10044241602 scopus 로고    scopus 로고
    • RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
    • DOI 10.1038/sj.emboj.7600449
    • Y. Akiyama, K. Kanehara, and K. Ito RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences EMBO J. 23 2004 4434 4442 (Pubitemid 39601968)
    • (2004) EMBO Journal , vol.23 , Issue.22 , pp. 4434-4442
    • Akiyama, Y.1    Kanehara, K.2    Ito, K.3
  • 72
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • DOI 10.1016/S1097-2765(03)00060-1
    • J.M. Flynn, S.B. Neher, Y.I. Kim, R.T. Sauer, and T.A. Baker Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals Mol. Cell 11 2003 671 683 (Pubitemid 36388762)
    • (2003) Molecular Cell , vol.11 , Issue.3 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.-I.3    Sauer, R.T.4    Baker, T.A.5
  • 73
    • 33846134757 scopus 로고    scopus 로고
    • E-mediated envelope stress response in Escherichia coli: Keys to graded, buffered, and rapid signal transduction
    • DOI 10.1101/gad.1496707
    • E-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction Genes Dev. 21 2007 124 136 (Pubitemid 46089713)
    • (2007) Genes and Development , vol.21 , Issue.1 , pp. 124-136
    • Chaba, R.1    Grigorova, I.L.2    Flynn, J.M.3    Baker, T.A.4    Gross, C.A.5
  • 75
    • 80655146194 scopus 로고    scopus 로고
    • e activity in Escherichia coli
    • E activity in Escherichia coli J. Bacteriol. 193 2011 6179 6186
    • (2011) J. Bacteriol. , vol.193 , pp. 6179-6186
    • Kulp, A.1    Kuehn, M.J.2
  • 77
    • 77952694508 scopus 로고    scopus 로고
    • Structural basis for the negative regulation of bacterial stress response by RseB
    • D.Y. Kim, E. Kwon, J. Choi, H.Y. Hwang, and K.K. Kim Structural basis for the negative regulation of bacterial stress response by RseB Protein Sci. 19 2010 1258 1263
    • (2010) Protein Sci. , vol.19 , pp. 1258-1263
    • Kim, D.Y.1    Kwon, E.2    Choi, J.3    Hwang, H.Y.4    Kim, K.K.5
  • 78
    • 14844309359 scopus 로고    scopus 로고
    • E- dependent response of Escherichia coli
    • DOI 10.1111/j.1365-2958.2005.04497.x
    • E-dependent response of Escherichia coli Mol. Microbiol. 55 2005 1403 1412 (Pubitemid 40342068)
    • (2005) Molecular Microbiology , vol.55 , Issue.5 , pp. 1403-1412
    • Tam, C.1    Missiakas, D.2
  • 79
    • 33846571920 scopus 로고    scopus 로고
    • SecY alterations that impair membrane protein folding and generate a membrane stress
    • DOI 10.1083/jcb.200611121
    • N. Shimohata, S. Nagamori, Y. Akiyama, H.R. Kaback, and K. Ito SecY alterations that impair membrane protein folding and generate a membrane stress J. Cell Biol. 176 2007 307 317 (Pubitemid 46184882)
    • (2007) Journal of Cell Biology , vol.176 , Issue.3 , pp. 307-317
    • Shimohata, N.1    Nagamori, S.2    Akiyama, Y.3    Kaback, H.R.4    Ito, K.5
  • 80
    • 33744950278 scopus 로고    scopus 로고
    • Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli
    • DOI 10.1074/jbc.M600819200
    • V. Douchin, C. Bohn, and P. Bouloc Down-regulation of porins by a small RNA bypasses the essentiality of the regulated intramembrane proteolysis protease RseP in Escherichia coli J. Biol. Chem. 281 2006 12253 12259 (Pubitemid 43855309)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12253-12259
    • Douchin, V.1    Bohn, C.2    Bouloc, P.3
  • 81
    • 7544239890 scopus 로고    scopus 로고
    • E envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA
    • DOI 10.1101/gad.1238604
    • E envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA Genes Dev. 18 2004 2686 2697 (Pubitemid 39453107)
    • (2004) Genes and Development , vol.18 , Issue.21 , pp. 2686-2697
    • Grigorova, I.L.1    Chaba, R.2    Zhong, H.J.3    Alba, B.M.4    Rhodius, V.5    Herman, C.6    Gross, C.A.7
  • 85
    • 0029878960 scopus 로고    scopus 로고
    • Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane
    • DOI 10.1074/jbc.271.17.10379
    • X. Hua, J. Sakai, M.S. Brown, and J.L. Goldstein Regulated cleavage of sterol regulatory element binding proteins requires sequences on both sides of the endoplasmic reticulum membrane J. Biol. Chem. 271 1996 10379 10384 (Pubitemid 26132526)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.17 , pp. 10379-10384
    • Hua, X.1    Sakai, J.2    Brown, M.S.3    Goldstein, J.L.4
  • 86
    • 0032504202 scopus 로고    scopus 로고
    • Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning
    • DOI 10.1074/jbc.273.28.17801
    • E. Duncan, U. Dave, J. Sakai, J. Goldstein, and M. Brown Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning J. Biol. Chem. 273 1998 17801 17809 (Pubitemid 28355124)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.28 , pp. 17801-17809
    • Duncan, E.A.1    Dave, U.P.2    Sakai, J.3    Goldstein, J.L.4    Brown, M.S.5
  • 87
    • 3142683280 scopus 로고    scopus 로고
    • W anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC
    • DOI 10.1111/j.1365-2958.2004.04031.x
    • W anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC Mol. Microbiol. 52 2004 1091 1105 (Pubitemid 38916176)
    • (2004) Molecular Microbiology , vol.52 , Issue.4 , pp. 1091-1105
    • Schobel, S.1    Zellmeier, S.2    Schumann, W.3    Wiegert, T.4
  • 88
    • 4143084775 scopus 로고    scopus 로고
    • Intramembrane proteolysis: Theme and variations
    • DOI 10.1126/science.1096187
    • M.S. Wolfe, and R. Kopan Intramembrane proteolysis: theme and variations Science 305 2004 1119 1123 (Pubitemid 39100316)
    • (2004) Science , vol.305 , Issue.5687 , pp. 1119-1123
    • Wolfe, M.S.1    Kopan, R.2
  • 89
    • 0024575242 scopus 로고
    • Switch protein alters specificity of RNA polymerase containing a compartment-specific sigma factor
    • L. Kroos, B. Kunkel, and R. Losick Switch protein alters specificity of RNA polymerase containing a compartment-specific sigma factor Science 243 1989 526 529 (Pubitemid 19048751)
    • (1989) Science , vol.243 , Issue.4890 , pp. 526-529
    • Kroos, L.1    Kunkel, B.2    Losick, R.3
  • 91
    • 44349189894 scopus 로고    scopus 로고
    • Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease
    • K. Koide, K. Ito, and Y. Akiyama Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease J. Biol. Chem. 283 2008 9562 9570
    • (2008) J. Biol. Chem. , vol.283 , pp. 9562-9570
    • Koide, K.1    Ito, K.2    Akiyama, Y.3
  • 92
    • 61549125968 scopus 로고    scopus 로고
    • Rhomboid protease dynamics and lipid interactions
    • A.N. Bondar, C. del Val, and S.H. White Rhomboid protease dynamics and lipid interactions Structure 17 2009 395 405
    • (2009) Structure , vol.17 , pp. 395-405
    • Bondar, A.N.1    Del Val, C.2    White, S.H.3
  • 93
    • 84863534125 scopus 로고    scopus 로고
    • An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency
    • Y. Zhou, S.M. Moin, S. Urban, and Y. Zhang An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency Structure 20 2012 1255 1263
    • (2012) Structure , vol.20 , pp. 1255-1263
    • Zhou, Y.1    Moin, S.M.2    Urban, S.3    Zhang, Y.4
  • 94
    • 33947498781 scopus 로고    scopus 로고
    • Environment of the active site region of RseP, an Escherichia coli regulated intramembrane proteolysis protease, assessed by site-directed cysteine alkylation
    • DOI 10.1074/jbc.M607339200
    • K. Koide, S. Maegawa, K. Ito, and Y. Akiyama Environment of the active site region of RseP, an Escherichia coli regulated intramembrane proteolysis protease, assessed by site-directed cysteine alkylation J. Biol. Chem. 282 2007 4553 4560 (Pubitemid 47100933)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4553-4560
    • Koide, K.1    Maegawa, S.2    Ito, K.3    Akiyama, Y.4
  • 95
    • 34248371981 scopus 로고    scopus 로고
    • Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease
    • DOI 10.1111/j.1365-2958.2007.05715.x
    • Y. Akiyama, and S. Maegawa Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease Mol. Microbiol. 64 2007 1028 1037 (Pubitemid 46743969)
    • (2007) Molecular Microbiology , vol.64 , Issue.4 , pp. 1028-1037
    • Akiyama, Y.1    Maegawa, S.2
  • 96
    • 34247370690 scopus 로고    scopus 로고
    • The intramembrane active site of GlpG, an E. Coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates
    • DOI 10.1111/j.1365-2958.2007.05679.x
    • S. Maegawa, K. Koide, K. Ito, and Y. Akiyama The intramembrane active site of GlpG, an E. coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates Mol. Microbiol. 64 2007 435 447 (Pubitemid 46632636)
    • (2007) Molecular Microbiology , vol.64 , Issue.2 , pp. 435-447
    • Maegawa, S.1    Koide, K.2    Ito, K.3    Akiyama, Y.4
  • 97
    • 35748974498 scopus 로고    scopus 로고
    • The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG
    • DOI 10.1016/j.jmb.2007.10.014, PII S0022283607013356
    • Y. Wang, S. Maegawa, Y. Akiyama, and Y. Ha The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG J. Mol. Biol. 374 2007 1104 1113 (Pubitemid 350052106)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.4 , pp. 1104-1113
    • Wang, Y.1    Maegawa, S.2    Akiyama, Y.3    Ha, Y.4
  • 98
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • K. Strisovsky, H.J. Sharpe, and M. Freeman Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates Mol. Cell 36 2009 1048 1059
    • (2009) Mol. Cell , vol.36 , pp. 1048-1059
    • Strisovsky, K.1    Sharpe, H.J.2    Freeman, M.3
  • 99
    • 35748982195 scopus 로고    scopus 로고
    • Cutting Proteins within Lipid Bilayers: Rhomboid Structure and Mechanism
    • DOI 10.1016/j.molcel.2007.12.003, PII S1097276507008350
    • M.K. Lemberg, and M. Freeman Cutting proteins within lipid bilayers: rhomboid structure and mechanism Mol. Cell 28 2007 930 940 (Pubitemid 350297031)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 930-940
    • Lemberg, M.K.1    Freeman, M.2
  • 100
    • 84878843045 scopus 로고    scopus 로고
    • Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics
    • S.M. Moin, and S. Urban Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics ELIFE 1 2012 e00173
    • (2012) ELIFE , vol.1 , pp. 00173
    • Moin, S.M.1    Urban, S.2
  • 102
    • 84860711067 scopus 로고    scopus 로고
    • Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S' subsites
    • Y. Xue, S. Chowdhury, X. Liu, Y. Akiyama, J. Ellman, and Y. Ha Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S' subsites Biochemistry 51 2012 3723 3731
    • (2012) Biochemistry , vol.51 , pp. 3723-3731
    • Xue, Y.1    Chowdhury, S.2    Liu, X.3    Akiyama, Y.4    Ellman, J.5    Ha, Y.6
  • 103
    • 84856292019 scopus 로고    scopus 로고
    • Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate
    • Y. Xue, and Y. Ha Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate J. Biol. Chem. 287 2012 3099 3107
    • (2012) J. Biol. Chem. , vol.287 , pp. 3099-3107
    • Xue, Y.1    Ha, Y.2
  • 104
    • 72049093490 scopus 로고    scopus 로고
    • Two proteolytic modules are involved in regulated intramembrane proteolysis of Bacillus subtilis RsiW
    • J. Heinrich, K. Hein, and T. Wiegert Two proteolytic modules are involved in regulated intramembrane proteolysis of Bacillus subtilis RsiW Mol. Microbiol. 74 2009 1412 1426
    • (2009) Mol. Microbiol. , vol.74 , pp. 1412-1426
    • Heinrich, J.1    Hein, K.2    Wiegert, T.3
  • 105
    • 84885087118 scopus 로고    scopus 로고
    • Function of site-2 proteases in bacteria and bacterial pathogens
    • (this issue)
    • J.S. Schneider, and M.S. Glickman Function of site-2 proteases in bacteria and bacterial pathogens BBA Biomemb. 1828 2013 2808 2814 (this issue)
    • (2013) BBA Biomemb. , vol.1828 , pp. 2808-2814
    • Schneider, J.S.1    Glickman, M.S.2
  • 106
    • 84885183980 scopus 로고    scopus 로고
    • The site-2 protease
    • (this issue)
    • R.B. Rawson The site-2 protease BBA Biomemb. 1828 2013 2801 2807 (this issue)
    • (2013) BBA Biomemb. , vol.1828 , pp. 2801-2807
    • Rawson, R.B.1
  • 107
    • 84880032415 scopus 로고    scopus 로고
    • Features of Pro-sigmaK important for cleavage by SpoIVFB, an intramembrane metalloprotease
    • (Epub ahead of print)
    • R. Zhou, K. Chen, X. Xiang, L. Gu, and L. Kroos Features of Pro-sigmaK important for cleavage by SpoIVFB, an intramembrane metalloprotease J. Bacteriol. 2013 (Epub ahead of print)
    • (2013) J. Bacteriol.
    • Zhou, R.1    Chen, K.2    Xiang, X.3    Gu, L.4    Kroos, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.