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Volumn 108, Issue 33, 2011, Pages 13740-13745

Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria

Author keywords

Intramembrane proteolysis; Signal sequence

Indexed keywords

BETA LACTAMASE; CELL PROTEIN; PROTEIN LEP; PROTEIN PRECURSOR; PROTEINASE; SIGNAL PEPTIDASE; SIGNAL PEPTIDE; SITE 2 PROTEASE; UNCLASSIFIED DRUG;

EID: 80052006484     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1108376108     Document Type: Article
Times cited : (54)

References (34)
  • 2
    • 0036809216 scopus 로고    scopus 로고
    • Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis
    • DOI 10.1016/S1097-2765(02)00655-X
    • Lemberg M.K., Martoglio B. (2002) Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis. Mol Cell 10:735-744. (Pubitemid 35335630)
    • (2002) Molecular Cell , vol.10 , Issue.4 , pp. 735-744
    • Lemberg, M.K.1    Martoglio, B.2
  • 3
    • 67649794833 scopus 로고    scopus 로고
    • Intramembrane proteolysis by signal peptide peptidases: A comparative discussion of GXGD-type aspartyl proteases
    • Fluhrer R., Steiner H., Haass C. (2009) Intramembrane proteolysis by signal peptide peptidases: A comparative discussion of GXGD-type aspartyl proteases. J Biol Chem 284:13975-13979.
    • (2009) J Biol Chem , vol.284 , pp. 13975-13979
    • Fluhrer, R.1    Steiner, H.2    Haass, C.3
  • 4
    • 77951226758 scopus 로고    scopus 로고
    • Signal peptide peptidase (SPP) assembles with substrates and misfolded membrane proteins into distinct oligomeric complexes
    • Schrul B., Kapp K., Sinning I., Dobberstein B. (2010) Signal peptide peptidase (SPP) assembles with substrates and misfolded membrane proteins into distinct oligomeric complexes. Biochem J 427:523-534.
    • (2010) Biochem J , vol.427 , pp. 523-534
    • Schrul, B.1    Kapp, K.2    Sinning, I.3    Dobberstein, B.4
  • 5
    • 67649827390 scopus 로고    scopus 로고
    • Intramembrane-cleaving proteases
    • Wolfe M.S. (2009) Intramembrane-cleaving proteases. J Biol Chem 284:13969-13973.
    • (2009) J Biol Chem , vol.284 , pp. 13969-13973
    • Wolfe, M.S.1
  • 6
    • 63649088506 scopus 로고    scopus 로고
    • Structure and mechanism of intramembrane protease
    • Ha Y. (2009) Structure and mechanism of intramembrane protease. Semin Cell Dev Biol 20:240-250.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 240-250
    • Ha, Y.1
  • 7
    • 0037304947 scopus 로고    scopus 로고
    • Intramembrane-cleaving proteases: Controlled liberation of proteins and bioactive peptides
    • DOI 10.1016/S0962-8924(02)00041-7, PII S0962892402000417
    • Weihofen A., Martoglio B. (2003) Intramembrane-cleaving proteases: Controlled liberation of proteins and bioactive peptides. Trends Cell Biol 13:71-78. (Pubitemid 36135888)
    • (2003) Trends in Cell Biology , vol.13 , Issue.2 , pp. 71-78
    • Weihofen, A.1    Martoglio, B.2
  • 8
    • 0037102458 scopus 로고    scopus 로고
    • YaeL (EcfE) activates the σ(E) pathway of stress response through a site-2 cleavage of anti-σ(E), RseA
    • (E), RseA. Genes Dev 16:2147-2155.
    • (2002) Genes Dev , vol.16 , pp. 2147-2155
    • Kanehara, K.1    Ito, K.2    Akiyama, Y.3
  • 9
    • 0037102509 scopus 로고    scopus 로고
    • DegS and YaeL participate sequentially in the cleavage of RseA to activate the σ(E)-dependent extracytoplasmic stress response
    • (E)-dependent extracytoplasmic stress response. Genes Dev 16:2156-2168.
    • (2002) Genes Dev , vol.16 , pp. 2156-2168
    • Alba, B.M.1    Leeds, J.A.2    Onufryk, C.3    Lu, C.Z.4    Gross, C.A.5
  • 10
    • 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
    • Walsh N.P., Alba B.M., Bose B., Gross C.A., 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. (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
  • 11
    • 10044241602 scopus 로고    scopus 로고
    • RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
    • DOI 10.1038/sj.emboj.7600449
    • Akiyama Y., Kanehara K., Ito K. (2004) RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences. EMBO J 23:4434-4442. (Pubitemid 39601968)
    • (2004) EMBO Journal , vol.23 , Issue.22 , pp. 4434-4442
    • Akiyama, Y.1    Kanehara, K.2    Ito, K.3
  • 12
    • 0022979418 scopus 로고
    • Molecular cloning and sequencing of the sppA gene and characterization of the encoded protease IV, a signal peptide peptidase, of Escherichia coli
    • Ichihara S., Suzuki T., Suzuki M., Mizushima S. (1986) Molecular cloning and sequencing of the sppA gene and characterization of the encoded protease IV, a signal peptide peptidase, of Escherichia coli. J Biol Chem 261:9405-9411. (Pubitemid 17218224)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.20 , pp. 9405-9411
    • Ichihara, S.1    Suzuki, T.2    Suzuki, M.3    Mizushima, S.4
  • 13
    • 45749095796 scopus 로고    scopus 로고
    • Escherichia coli signal peptide peptidase A is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the S49 protease family
    • DOI 10.1021/bi800657p
    • Wang P., et al. (2008) Escherichia coli signal peptide peptidase A is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the S49 protease family. Biochemistry 47:6361-6369. (Pubitemid 351874227)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6361-6369
    • Wang, P.1    Shim, E.2    Cravatt, B.3    Jacobsen, R.4    Schoeniger, J.5    Kim, A.C.6    Paetzel, M.7    Dalbey, R.E.8
  • 14
    • 0024526131 scopus 로고
    • Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli
    • Inada T., Court D.L., Ito K., Nakamura Y. (1989) Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli. J Bacteriol 171:585-587.
    • (1989) J Bacteriol , vol.171 , pp. 585-587
    • Inada, T.1    Court, D.L.2    Ito, K.3    Nakamura, Y.4
  • 15
    • 0023177156 scopus 로고
    • Characterization of the sppA gene coding for protease IV, a signal peptide peptidase of Escherichia coli
    • Suzuki T., Itoh A., Ichihara S., MizushimaS. (1987) Characterizationof the sppAgene coding for protease IV, a signal peptide peptidase of Escherichia coli. J Bacteriol 169:2523-2528. (Pubitemid 17104310)
    • (1987) Journal of Bacteriology , vol.169 , Issue.6 , pp. 2523-2528
    • Suzuki, T.1    Itoh, A.2    Ichihara, S.3    Mizushima, S.4
  • 16
    • 0023757506 scopus 로고
    • Degradation of a signal peptide by protease IV and oligopeptidase A
    • Novak P., Dev I.K. (1988) Degradation of a signal peptide by protease IV and oligopeptidase A. J Bacteriol 170:5067-5075. (Pubitemid 18259455)
    • (1988) Journal of Bacteriology , vol.170 , Issue.11 , pp. 5067-5075
    • Novak, P.1    Dev, I.K.2
  • 17
    • 33750381048 scopus 로고    scopus 로고
    • The bacterial twin-arginine translocation pathway
    • DOI 10.1146/annurev.micro.60.080805.142212
    • Lee P.A., Tullman-Ercek D., Georgiou G. (2006) The bacterial twin-arginine translocation pathway. Annu Rev Microbiol 60:373-395. (Pubitemid 44627954)
    • (2006) Annual Review of Microbiology , vol.60 , pp. 373-395
    • Lee, P.A.1    Tullman-Ercek, D.2    Georgiou, G.3
  • 18
    • 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
    • Schöbel S., Zellmeier S., Schumann W., Wiegert T. (2004) The Bacillus subtilis sigmaW anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC. Mol Microbiol 52:1091-1105. (Pubitemid 38916176)
    • (2004) Molecular Microbiology , vol.52 , Issue.4 , pp. 1091-1105
    • Schobel, S.1    Zellmeier, S.2    Schumann, W.3    Wiegert, T.4
  • 19
    • 51149117340 scopus 로고    scopus 로고
    • The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP
    • Heinrich J., Lundén T., Kontinen V.P.,Wiegert T. (2008) The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP.Microbiology 154:1989-1997.
    • (2008) Microbiology , vol.154 , pp. 1989-1997
    • Heinrich, J.1    Lundén, T.2    Kontinen, V.P.3    Wiegert, T.4
  • 20
    • 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
    • An F.Y., Sulavik M.C., Clewell D.B. (1999) 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 181:5915-5921. (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
  • 21
    • 38949108711 scopus 로고    scopus 로고
    • Characterization of the sequence specificity determinants required for processing and control of sex pheromone by the intramembrane protease Eep and the plasmid-encoded protein PrgY
    • DOI 10.1128/JB.01327-07
    • Chandler J.R., Dunny G.M. (2008) Characterization of the sequence specificity determinants required for processing and control of sex pheromone by the intramembrane protease Eep and the plasmid-encoded protein PrgY. J Bacteriol 190:1172-1183. (Pubitemid 351214998)
    • (2008) Journal of Bacteriology , vol.190 , Issue.4 , pp. 1172-1183
    • Chandler, J.R.1    Dunny, G.M.2
  • 22
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
    • DOI 10.1016/S1534-5807(02)00203-4
    • Shen J., Chen X., Hendershot L., Prywes R. (2002) ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 3:99-111. (Pubitemid 34778399)
    • (2002) Developmental Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 23
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • Von Heijne G. (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 133:17-21.24.
    • (1983) Eur J Biochem , vol.133
    • Von Heijne, G.1
  • 24
    • 38349192547 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptide peptidase
    • Kim A.C., Oliver D.C., Paetzel M. (2008) Crystal structure of a bacterial signal peptide peptidase. J Mol Biol 376:352-366.
    • (2008) J Mol Biol , vol.376 , pp. 352-366
    • Kim, A.C.1    Oliver, D.C.2    Paetzel, M.3
  • 25
    • 33745207334 scopus 로고    scopus 로고
    • Signal peptide peptidase is required for dislocation from the endoplasmic reticulum
    • Loureiro J., et al. (2006) Signal peptide peptidase is required for dislocation from the endoplasmic reticulum. Nature 441:894-897.
    • (2006) Nature , vol.441 , pp. 894-897
    • Loureiro, J.1
  • 26
    • 9444239782 scopus 로고    scopus 로고
    • A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase
    • DOI 10.1042/BJ20041216
    • Crawshaw S.G., Martoglio B., Meacock S.L., High S. (2004) A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase. Biochem J 384:9-17. (Pubitemid 39564156)
    • (2004) Biochemical Journal , vol.384 , Issue.1 , pp. 9-17
    • Crawshaw, S.G.1    Martoglio, B.2    Meacock, S.L.3    High, S.4
  • 27
    • 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
    • Kanehara K., Ito K., Akiyama Y. (2003) YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA. EMBO J 22:6389-6398. (Pubitemid 37522595)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6389-6398
    • Kanehara, K.1    Ito, K.2    Akiyama, Y.3
  • 28
    • 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
    • Grigorova I.L., et al. (2004) Fine-tuning of the Escherichia coli sigmaE envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA. Genes Dev 18:2686-2697. (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
  • 29
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • DOI 10.1126/science.1150755
    • Feng L., et al. (2007) Structure of a site-2 protease family intramembrane metalloprotease. Science 318:1608-1612. (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
  • 30
    • 58049199407 scopus 로고    scopus 로고
    • A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli
    • Inaba K., et al. (2008) A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli. J Biol Chem 283:35042-35052.
    • (2008) J Biol Chem , vol.283 , pp. 35042-35052
    • Inaba, K.1
  • 31
    • 70349299921 scopus 로고    scopus 로고
    • Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage
    • Li X., et al. (2009) Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage. Proc Natl Acad Sci USA 106:14837-14842.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14837-14842
    • Li, X.1
  • 32
    • 0028912195 scopus 로고
    • Product of a new gene, syd, functionally interacts with SecY when overproduced in Escherichia coli
    • Shimoike T., et al. (1995) Product of a new gene, syd, functionally interacts with SecY when overproduced in Escherichia coli. J Biol Chem 270:5519-5526.
    • (1995) J Biol Chem , vol.270 , pp. 5519-5526
    • Shimoike, T.1
  • 33
    • 0026701330 scopus 로고
    • Effects of total hydrophobicity and length of the hydrophobic domain of a signal peptide on in vitro translocation efficiency
    • Hikita C., Mizushima S. (1992) Effects of total hydrophobicity and length of the hydrophobic domain of a signal peptide on in vitro translocation efficiency. J Biol Chem 267:4882-4888.
    • (1992) J Biol Chem , vol.267 , pp. 4882-4888
    • Hikita, C.1    Mizushima, S.2
  • 34
    • 0037226762 scopus 로고    scopus 로고
    • Biochemical characterization of a mutationally altered protein translocase: Proton motive force stimulation of the initiation phase of translocation
    • DOI 10.1128/JB.185.2.405-412.2003
    • Mori H., Ito K. (2003) Biochemical characterization of a mutationally altered protein translocase: Proton motive force stimulation of the initiation phase of translocation. J Bacteriol 185:405-412. (Pubitemid 36070465)
    • (2003) Journal of Bacteriology , vol.185 , Issue.2 , pp. 405-412
    • Mori, H.1    Ito, K.2


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