메뉴 건너뛰기




Volumn 6, Issue 6, 1997, Pages 1129-1138

The chemistry and enzymology of the type I signal peptidases

Author keywords

Endoplasmic reticulum; Leader peptidase; Membrane protein; Protein secretion; Signal peptidase

Indexed keywords

MEMBRANE ENZYME; SIGNAL PEPTIDASE; SIGNAL PEPTIDE;

EID: 0030998468     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060601     Document Type: Review
Times cited : (219)

References (104)
  • 1
    • 0029592701 scopus 로고
    • Determination of a 17,484 bp nucleotide sequence around the 39 degrees region of the Bacillus subtilis chromosome and similarity analysis of the products of putative ORFs
    • Akagawa E, Kurita K, Sugawara T, Nakamura K, Kasahara Y, Ogasawara N, Yamane K. 1995. Determination of a 17,484 bp nucleotide sequence around the 39 degrees region of the Bacillus subtilis chromosome and similarity analysis of the products of putative ORFs. Microbiology 141:3241-3245.
    • (1995) Microbiology , vol.141 , pp. 3241-3245
    • Akagawa, E.1    Kurita, K.2    Sugawara, T.3    Nakamura, K.4    Kasahara, Y.5    Ogasawara, N.6    Yamane, K.7
  • 3
    • 0023667725 scopus 로고
    • Purification and characterization of chicken oviduct microsomal signal peptidase
    • Baker RK, Lively MO. 1987. Purification and characterization of chicken oviduct microsomal signal peptidase. Biochemistry 26:8561-8567.
    • (1987) Biochemistry , vol.26 , pp. 8561-8567
    • Baker, R.K.1    Lively, M.O.2
  • 4
    • 0026503688 scopus 로고
    • Synthesis of precursor maltosebinding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo
    • Barkocy-Gallagher GA, Bassford PJ Jr. 1992. Synthesis of precursor maltosebinding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo. J Biol Chem 267:1231-1238.
    • (1992) J Biol Chem , vol.267 , pp. 1231-1238
    • Barkocy-Gallagher, G.A.1    Bassford Jr., P.J.2
  • 5
    • 0018427455 scopus 로고
    • Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm
    • Bassford P, Beckwith J. 1979. Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm. Nature 277:538-541.
    • (1979) Nature , vol.277 , pp. 538-541
    • Bassford, P.1    Beckwith, J.2
  • 6
    • 0018935901 scopus 로고
    • Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli
    • Bedouelle H, Bassford PJ Jr, Fowler AV, Zabin I, Beckwith J, Hofnung M. 1980. Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli. Nature 285:78-81.
    • (1980) Nature , vol.285 , pp. 78-81
    • Bedouelle, H.1    Bassford Jr., P.J.2    Fowler, A.V.3    Zabin, I.4    Beckwith, J.5    Hofnung, M.6
  • 7
    • 0025769806 scopus 로고
    • Mitochondrial inner membrane peptidase 1 of Saccharomyces cerevisiae shows sequence similarity to the Escherichia coli leader peptidase
    • Behrens M, Michaelis G, Pratje E. 1991. Mitochondrial inner membrane peptidase 1 of Saccharomyces cerevisiae shows sequence similarity to the Escherichia coli leader peptidase. Mol Gen Genet 228:167-176.
    • (1991) Mol Gen Genet , vol.228 , pp. 167-176
    • Behrens, M.1    Michaelis, G.2    Pratje, E.3
  • 8
    • 0025046731 scopus 로고
    • Mapping of catalytically important domains in Escherichia coli leader peptidase
    • Bilgin N, Lee JI, Zhu HY, Dalbey RE, von Heijne G. 1990. Mapping of catalytically important domains in Escherichia coli leader peptidase. EMBO J 9:2717-2722.
    • (1990) EMBO J , vol.9 , pp. 2717-2722
    • Bilgin, N.1    Lee, J.I.2    Zhu, H.Y.3    Dalbey, R.E.4    Von Heijne, G.5
  • 9
    • 0026606345 scopus 로고
    • On the catalytic mechanism of prokaryotic leader peptidase 1
    • Black MT, Munn JG, Allsop AE. 1992. On the catalytic mechanism of prokaryotic leader peptidase 1. Biochem J 282:539-543.
    • (1992) Biochem J , vol.282 , pp. 539-543
    • Black, M.T.1    Munn, J.G.2    Allsop, A.E.3
  • 10
    • 0027291327 scopus 로고
    • Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad
    • Black MT. 1993. Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad. J Bacteriol 175:4957-4961.
    • (1993) J Bacteriol , vol.175 , pp. 4957-4961
    • Black, M.T.1
  • 11
    • 0023894180 scopus 로고
    • SEC11 is required for signal peptide processing and yeast cell growth
    • Böhni PC, Deshaies RJ, Schekman RW. 1988. SEC11 is required for signal peptide processing and yeast cell growth. J Cell Biol 106:1035-1042.
    • (1988) J Cell Biol , vol.106 , pp. 1035-1042
    • Böhni, P.C.1    Deshaies, R.J.2    Schekman, R.W.3
  • 12
    • 0029809574 scopus 로고    scopus 로고
    • Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I
    • Bolhuis A, Sorokin A, Azevedo V, Ehrlich SD, Braun PG, de Jong A, Venema G, Bron S, van Dijl JM. 1996. Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I. Mol Microbiol 22:605-618.
    • (1996) Mol Microbiol , vol.22 , pp. 605-618
    • Bolhuis, A.1    Sorokin, A.2    Azevedo, V.3    Ehrlich, S.D.4    Braun, P.G.5    De Jong, A.6    Venema, G.7    Bron, S.8    Van Dijl, J.M.9
  • 14
    • 0020078214 scopus 로고
    • Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase
    • Carlson M, Botstein D. 1982. Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28:145-154.
    • (1982) Cell , vol.28 , pp. 145-154
    • Carlson, M.1    Botstein, D.2
  • 17
    • 0029796449 scopus 로고    scopus 로고
    • Molecular cloning and expression of the spsB gene encoding an essential type I signal peptidase from Staphylococcus aureus
    • Cregg KM, Wilding EI, Black MT. 1996. Molecular cloning and expression of the spsB gene encoding an essential type I signal peptidase from Staphylococcus aureus. J Bacteriol 178:5712-5718.
    • (1996) J Bacteriol , vol.178 , pp. 5712-5718
    • Cregg, K.M.1    Wilding, E.I.2    Black, M.T.3
  • 18
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes - A new protease family
    • Dalbey RE, von Heijne G. 1992. Signal peptidases in prokaryotes and eukaryotes - A new protease family. Trends Biochem Sci 17:474-478.
    • (1992) Trends Biochem Sci , vol.17 , pp. 474-478
    • Dalbey, R.E.1    Von Heijne, G.2
  • 19
    • 0022400507 scopus 로고
    • Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane
    • Dalbey RE, Wickner W. 1985. Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane J Biol Chem 260:15925-15931.
    • (1985) J Biol Chem , vol.260 , pp. 15925-15931
    • Dalbey, R.E.1    Wickner, W.2
  • 20
    • 0020584151 scopus 로고
    • Demonstration by a novel genetic technique that leader peptidase is an essential enzyme of Escherichia coli
    • Date T. 1983. Demonstration by a novel genetic technique that leader peptidase is an essential enzyme of Escherichia coli. J Bacteriol 154:76-83.
    • (1983) J Bacteriol , vol.154 , pp. 76-83
    • Date, T.1
  • 21
    • 0012295399 scopus 로고
    • Isolation of the Escherichia coli leader peptidase gene and effects of leader peptidase overproduction in vivo
    • Date T, Wickner W. 1981. Isolation of the Escherichia coli leader peptidase gene and effects of leader peptidase overproduction in vivo. Proc Natl Acad Sci USA 78:6106-6110.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6106-6110
    • Date, T.1    Wickner, W.2
  • 22
    • 0025202766 scopus 로고
    • Minimum substrate sequence for signal peptidase I of Escherichia coli
    • Dev IK, Ray PH, Novak P. 1990. Minimum substrate sequence for signal peptidase I of Escherichia coli. J Biol Chem 265:20069-20072.
    • (1990) J Biol Chem , vol.265 , pp. 20069-20072
    • Dev, I.K.1    Ray, P.H.2    Novak, P.3
  • 23
    • 0022671355 scopus 로고
    • Requirements for substrate recognition by bacterial leader peptidase
    • Dierstein R, Wickner W. 1986. Requirements for substrate recognition by bacterial leader peptidase. EMBO J 5:427-431.
    • (1986) EMBO J , vol.5 , pp. 427-431
    • Dierstein, R.1    Wickner, W.2
  • 24
    • 0018236650 scopus 로고
    • Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein
    • Emr SD, Schwanz M, Silhavy TJ. 1978. Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein. Proc Natl Acad Sci USA 75:5802-5806.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5802-5806
    • Emr, S.D.1    Schwanz, M.2    Silhavy, T.J.3
  • 25
    • 0019332779 scopus 로고
    • Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor
    • Emr SD, Silhavy TJ. 1980. Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor. J Mol Biol 147:63-90.
    • (1980) J Mol Biol , vol.147 , pp. 63-90
    • Emr, S.D.1    Silhavy, T.J.2
  • 26
    • 0012295328 scopus 로고
    • Purification of microsomal signal peptidase as a complex
    • Evans EA, Gilmore R, Blobel G. 1986. Purification of microsomal signal peptidase as a complex. Proc Natl Acad Sci USA 83:581-585.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 581-585
    • Evans, E.A.1    Gilmore, R.2    Blobel, G.3
  • 27
    • 0029927143 scopus 로고    scopus 로고
    • The homologue of the mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae
    • Fang H, Panzner S, Mullins C, Hartmann E, Green N. 1996. The homologue of the mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae. J Biol Chem 277:16460-16465.
    • (1996) J Biol Chem , vol.277 , pp. 16460-16465
    • Fang, H.1    Panzner, S.2    Mullins, C.3    Hartmann, E.4    Green, N.5
  • 28
    • 0025216609 scopus 로고
    • Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site
    • Fikes JD, Barkocy-Gallagher GA, Klapper DG, Bassford PJ Jr. 1990. Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site. J Biol Chem 265:3417-3423.
    • (1990) J Biol Chem , vol.265 , pp. 3417-3423
    • Fikes, J.D.1    Barkocy-Gallagher, G.A.2    Klapper, D.G.3    Bassford Jr., P.J.4
  • 29
    • 0023177150 scopus 로고
    • Export of unprocessed precursor maltose-binding protein to the periplasm of Escherichia coli cells
    • Fikes JD, Bassford PJ Jr. 1987. Export of unprocessed precursor maltose-binding protein to the periplasm of Escherichia coli cells. J Bacteriol 769:2352-2359.
    • (1987) J Bacteriol , vol.769 , pp. 2352-2359
    • Fikes, J.D.1    Bassford Jr., P.J.2
  • 31
    • 0023911277 scopus 로고
    • Substrate specificity of eukaryotic signal peptidase. Site-saturation mutagenesis at position - 1 regulates cleavage between multiple sites in human pre (delta pro) apolipoprotein A-II
    • Folz RJ, Nothwehr SF, Gordon JI. 1988. Substrate specificity of eukaryotic signal peptidase. Site-saturation mutagenesis at position - 1 regulates cleavage between multiple sites in human pre (delta pro) apolipoprotein A-II. J Biol Chem 263:2070-2078.
    • (1988) J Biol Chem , vol.263 , pp. 2070-2078
    • Folz, R.J.1    Nothwehr, S.F.2    Gordon, J.I.3
  • 34
    • 0028142990 scopus 로고
    • cDNA-derived primary structure of the 25-kDa subunit of canine microsomal signal peptidase complex
    • Greenburg G, Blobel G. 1994. cDNA-derived primary structure of the 25-kDa subunit of canine microsomal signal peptidase complex. J Biol Chem 269:25354-25358.
    • (1994) J Biol Chem , vol.269 , pp. 25354-25358
    • Greenburg, G.1    Blobel, G.2
  • 35
    • 0024428204 scopus 로고
    • A subunit of mammalian signal peptidase is homologous to yeast SEC11 protein
    • Greenburg G, Shelness GS, Blobel G. 1989. A subunit of mammalian signal peptidase is homologous to yeast SEC11 protein. J Biol Chem 264:15762-15765
    • (1989) J Biol Chem , vol.264 , pp. 15762-15765
    • Greenburg, G.1    Shelness, G.S.2    Blobel, G.3
  • 36
    • 0024852098 scopus 로고
    • The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical
    • Halpin C, Elderfield PD, James HE, Zimmermann R, Dunbar B, Robinson C. 1989. The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical. EMBO J 8:3917-3921.
    • (1989) EMBO J , vol.8 , pp. 3917-3921
    • Halpin, C.1    Elderfield, P.D.2    James, H.E.3    Zimmermann, R.4    Dunbar, B.5    Robinson, C.6
  • 37
    • 0018380264 scopus 로고
    • De novo biosynthesis of an enzymatically active precursor form of bovine pancreatic RNase
    • Haugen TH, Heath EC. 1979. De novo biosynthesis of an enzymatically active precursor form of bovine pancreatic RNase. Proc Natl Acad Sci USA 76:2689-2693.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 2689-2693
    • Haugen, T.H.1    Heath, E.C.2
  • 38
    • 0028886749 scopus 로고
    • Bacillus amyloliquefaciens possesses a second type I signal peptidase with extensive sequence similarity to other Bacillus Spases
    • Hoang V, Hofemeister J. 1995. Bacillus amyloliquefaciens possesses a second type I signal peptidase with extensive sequence similarity to other Bacillus Spases. Biochim Biophys Acta 1269:64-68.
    • (1995) Biochim Biophys Acta , vol.1269 , pp. 64-68
    • Hoang, V.1    Hofemeister, J.2
  • 39
    • 0024526131 scopus 로고
    • Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli
    • Inada T, Court DL, Ito K, Nakamura Y. 1989. Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli. J Bacteriol 177:585-587.
    • (1989) J Bacteriol , vol.177 , pp. 585-587
    • Inada, T.1    Court, D.L.2    Ito, K.3    Nakamura, Y.4
  • 40
    • 0020453357 scopus 로고
    • Purification of the precursor form of maltose-binding protein, a periplasmic protein of Escherichia coli
    • Ito K. 1982. Purification of the precursor form of maltose-binding protein, a periplasmic protein of Escherichia coli. J Biol Chem 257:9895-9897.
    • (1982) J Biol Chem , vol.257 , pp. 9895-9897
    • Ito, K.1
  • 41
    • 0020980478 scopus 로고
    • Quantitative assay for signal peptidase
    • Jackson RC. 1983. Quantitative assay for signal peptidase. Methods Enzymol 96:784-794.
    • (1983) Methods Enzymol , vol.96 , pp. 784-794
    • Jackson, R.C.1
  • 42
    • 0017636299 scopus 로고
    • Post-translational cleavage of presecretory proteins with an extract of rough microsomes from canine pancreas containing signal peptidase activity
    • Jackson RC, Blobel G. 1977. Post-translational cleavage of presecretory proteins with an extract of rough microsomes from canine pancreas containing signal peptidase activity. Proc Natl Acad Sci USA 74:5598-5602.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5598-5602
    • Jackson, R.C.1    Blobel, G.2
  • 43
    • 0018895021 scopus 로고
    • Post-translational processing of full-length presecretory proteins with canine pancreatic signal peptidase
    • Jackson RC, Blobel G. 1980. Post-translational processing of full-length presecretory proteins with canine pancreatic signal peptidase. Ann NY Acad Sci 343:391-404.
    • (1980) Ann NY Acad Sci , vol.343 , pp. 391-404
    • Jackson, R.C.1    Blobel, G.2
  • 44
    • 0019876659 scopus 로고
    • Phospholipid is required for the processing of presecretory proteins by detergent-solubilized canine pancreatic signal peptidase
    • Jackson RC, White WR. 1981. Phospholipid is required for the processing of presecretory proteins by detergent-solubilized canine pancreatic signal peptidase. J Biol Chem 256:2545-2550.
    • (1981) J Biol Chem , vol.256 , pp. 2545-2550
    • Jackson, R.C.1    White, W.R.2
  • 45
    • 0030063873 scopus 로고    scopus 로고
    • Membrane topology of the 12- and 25-kDa subunits of the mammalian signal peptidase complex
    • Kalies KU, Hartmann E. 1996. Membrane topology of the 12- and 25-kDa subunits of the mammalian signal peptidase complex. J Biol Chem 271:3925-3929.
    • (1996) J Biol Chem , vol.271 , pp. 3925-3929
    • Kalies, K.U.1    Hartmann, E.2
  • 46
    • 0018124520 scopus 로고
    • Processing of prepromelittin by subcellular fractions from rat liver
    • Kaschnitz R, Kreil G. 1978. Processing of prepromelittin by subcellular fractions from rat liver. Biochem Biophys Res Commun 83:901-907.
    • (1978) Biochem Biophys Res Commun , vol.83 , pp. 901-907
    • Kaschnitz, R.1    Kreil, G.2
  • 47
    • 0023646043 scopus 로고
    • Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis
    • Kirwin PM, Elderfield PD, Robinson C. 1987. Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis. J Biol Chem 262:16386-16390.
    • (1987) J Biol Chem , vol.262 , pp. 16386-16390
    • Kirwin, P.M.1    Elderfield, P.D.2    Robinson, C.3
  • 48
    • 0020371938 scopus 로고
    • Diverse effects of mutations in the signal sequence on the secretion of beta-lactamase in Salmonella typhimurium
    • Koshland D, Sauer RT, Botstein D. 1982. Diverse effects of mutations in the signal sequence on the secretion of beta-lactamase in Salmonella typhimurium. Cell 30:903-914.
    • (1982) Cell , vol.30 , pp. 903-914
    • Koshland, D.1    Sauer, R.T.2    Botstein, D.3
  • 49
    • 0022343605 scopus 로고
    • Conserved residues of the leader peptide are essential for cleavage by leader peptidase
    • Kuhn A, Wickner W. 1985. Conserved residues of the leader peptide are essential for cleavage by leader peptidase. J Biol Chem 260:15914-15918.
    • (1985) J Biol Chem , vol.260 , pp. 15914-15918
    • Kuhn, A.1    Wickner, W.2
  • 50
    • 0028103847 scopus 로고
    • Determination of the kinetic parameters of Escherichia coli leader peptidase activity using a continuous assay: The pH dependence and time-dependent inhibition by beta-lactams are consistent with a novel serine protease mechanism
    • Kuo D, Weidner J, Griffin P, Shah SK, Knight WB. 1994. Determination of the kinetic parameters of Escherichia coli leader peptidase activity using a continuous assay: The pH dependence and time-dependent inhibition by beta-lactams are consistent with a novel serine protease mechanism. Biochemistry 33:8347-8354.
    • (1994) Biochemistry , vol.33 , pp. 8347-8354
    • Kuo, D.1    Weidner, J.2    Griffin, P.3    Shah, S.K.4    Knight, W.B.5
  • 51
    • 0027287556 scopus 로고
    • Escherichia coli leader peptidase: Production of an active form lacking a requirement for detergent and development of peptide substrates
    • Kuo DW, Chan HK, Wilson CJ, Griffin PR, Williams H, Knight WB. 1993. Escherichia coli leader peptidase: Production of an active form lacking a requirement for detergent and development of peptide substrates. Arch Biochem Biophys 303:274-280.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 274-280
    • Kuo, D.W.1    Chan, H.K.2    Wilson, C.J.3    Griffin, P.R.4    Williams, H.5    Knight, W.B.6
  • 52
    • 0024832465 scopus 로고
    • Autodigestion and RecA-dependent cleavage of Indmutant LexA proteins
    • Lin LL, Little JW. 1989. Autodigestion and RecA-dependent cleavage of Indmutant LexA proteins. J Mol Biol 210:439-452.
    • (1989) J Mol Biol , vol.210 , pp. 439-452
    • Lin, L.L.1    Little, J.W.2
  • 53
    • 0027214683 scopus 로고
    • LexA cleavage and other self-processing reactions
    • Little JW. 1993. LexA cleavage and other self-processing reactions. J Bacteriol 175:4943-4950.
    • (1993) J Bacteriol , vol.175 , pp. 4943-4950
    • Little, J.W.1
  • 55
    • 0021099785 scopus 로고
    • Hen oviduct signal peptidase is an integral membrane protein
    • Lively MO, Walsh KA. 1983. Hen oviduct signal peptidase is an integral membrane protein. J Biol Chem 255:9488-9495.
    • (1983) J Biol Chem , vol.255 , pp. 9488-9495
    • Lively, M.O.1    Walsh, K.A.2
  • 56
    • 0029049360 scopus 로고
    • The endogenous Bacillus subtilis (natto) plasmids pTA1015 and pTA1040 contain signal peptidase-encoding genes: Identification of a new structural module on cryptic plasmids
    • Meijer WJJ, de Jong A, Wisman GBA, Tjalsma H, Venema G, Bron S, van Dijl JM. 1995. The endogenous Bacillus subtilis (natto) plasmids pTA1015 and pTA1040 contain signal peptidase-encoding genes: Identification of a new structural module on cryptic plasmids. Mol Microbiol 17:621-631.
    • (1995) Mol Microbiol , vol.17 , pp. 621-631
    • Meijer, W.J.J.1    De Jong, A.2    Wisman, G.B.A.3    Tjalsma, H.4    Venema, G.5    Bron, S.6    Van Dijl, J.M.7
  • 57
    • 0020390269 scopus 로고
    • Mechanism of incorporation of cell envelope proteins in Escherichia coli
    • Michaelis S, Beckwith J. 1982. Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu Rev Microbiol 36:435-465.
    • (1982) Annu Rev Microbiol , vol.36 , pp. 435-465
    • Michaelis, S.1    Beckwith, J.2
  • 59
    • 0023664531 scopus 로고
    • A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli
    • Moore KE, Miura S. 1987. A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli. J Biol Chem 262:8806-8813.
    • (1987) J Biol Chem , vol.262 , pp. 8806-8813
    • Moore, K.E.1    Miura, S.2
  • 60
    • 0029558402 scopus 로고
    • A TnphoA insertion within the Bradyrhizobium japonicum sipS gene, homologous to prokaryolic signal peptidases, results in extensive changes in the expression of PBM-specific nodulins of infected soybean (Glycine max) cells
    • Müller P, Ahrens K, Keller T, Klaucke A. 1995. A TnphoA insertion within the Bradyrhizobium japonicum sipS gene, homologous to prokaryolic signal peptidases, results in extensive changes in the expression of PBM-specific nodulins of infected soybean (Glycine max) cells. Mol Microbiol 18:831-840.
    • (1995) Mol Microbiol , vol.18 , pp. 831-840
    • Müller, P.1    Ahrens, K.2    Keller, T.3    Klaucke, A.4
  • 61
    • 0029146856 scopus 로고
    • A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae
    • Mullins C, Lu YQ, Campbell A, Fang H, Green N. 1995. A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae. J Biol Chem 270:17139-17147.
    • (1995) J Biol Chem , vol.270 , pp. 17139-17147
    • Mullins, C.1    Lu, Y.Q.2    Campbell, A.3    Fang, H.4    Green, N.5
  • 62
    • 0029799885 scopus 로고    scopus 로고
    • Structurally related Spclp and Spc2p of yeast signal peptidase complex are functionally distinct
    • Mullins C, Meyers HM, Hartmann E, Green N, Fang H. 1996. Structurally related Spclp and Spc2p of yeast signal peptidase complex are functionally distinct. J Biol Chem 271:29094-29099.
    • (1996) J Biol Chem , vol.271 , pp. 29094-29099
    • Mullins, C.1    Meyers, H.M.2    Hartmann, E.3    Green, N.4    Fang, H.5
  • 63
    • 0026583534 scopus 로고
    • Molecular cloning of a cDNA encoding the glycoprotein of hen oviduct microsomal signal peptidase
    • Newsome AL, McLean JW, Lively MO. 1992. Molecular cloning of a cDNA encoding the glycoprotein of hen oviduct microsomal signal peptidase. Biochem J 282:447-452.
    • (1992) Biochem J , vol.282 , pp. 447-452
    • Newsome, A.L.1    McLean, J.W.2    Lively, M.O.3
  • 64
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G. 1996a. Identification of prokaryotic and eukaryotic signal peptides and prediction of cleavage sites. Protein Engineering 10:1-6.
    • (1996) Protein Engineering , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 65
    • 0029868212 scopus 로고    scopus 로고
    • Defining a similarity threshold for a functional protein sequence pattern: The signal peptide cleavage site
    • Nielsen H, Engelbrecht J, von Heijne G, Brunak S. 1996b. Defining a similarity threshold for a functional protein sequence pattern: The signal peptide cleavage site. Proteins Struct Func Genet 24:165-177.
    • (1996) Proteins Struct Func Genet , vol.24 , pp. 165-177
    • Nielsen, H.1    Engelbrecht, J.2    Von Heijne, G.3    Brunak, S.4
  • 66
    • 0026507687 scopus 로고
    • A signal peptide with a proline next to the cleavage site inhibits leader peptidase when present in a sec-independent protein
    • Nilsson I, von Heijne G. 1992. A signal peptide with a proline next to the cleavage site inhibits leader peptidase when present in a sec-independent protein. FEBS Lett 299:243-246.
    • (1992) FEBS Lett , vol.299 , pp. 243-246
    • Nilsson, I.1    Von Heijne, G.2
  • 67
    • 0027752461 scopus 로고
    • A mitochondrial protease with two calalylic subunits of nonoverlapping specificities
    • Nunnari J, Fox TD, Walter P. 1993. A mitochondrial protease with two calalylic subunits of nonoverlapping specificities. Science 262:1997-2004.
    • (1993) Science , vol.262 , pp. 1997-2004
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 68
    • 0029106404 scopus 로고
    • Cloning and sequence analysis of a signal peptidase I from the thermophilic cyanobacterium Phormidium laminosum
    • Packer JC, Andre D, Howe CJ. 1995. Cloning and sequence analysis of a signal peptidase I from the thermophilic cyanobacterium Phormidium laminosum. Plant Mol Biol 27:199-204.
    • (1995) Plant Mol Biol , vol.27 , pp. 199-204
    • Packer, J.C.1    Andre, D.2    Howe, C.J.3
  • 72
    • 0022730631 scopus 로고
    • One nuclear gene controls the removal of transient pre-sequences from two yeast proteins: One encoded by the nuclear the other by the mitochondrial genome
    • Pratje E, Guiard B. 1986. One nuclear gene controls the removal of transient pre-sequences from two yeast proteins: One encoded by the nuclear the other by the mitochondrial genome. EMBO J 5:1313-1317.
    • (1986) EMBO J , vol.5 , pp. 1313-1317
    • Pratje, E.1    Guiard, B.2
  • 73
    • 0027471438 scopus 로고
    • Human coagulation factor X deficiency caused by a mutant signal peptide that blocks cleavage by signal peptidase but not targeting and translocation to the endoplasmic reticulum
    • Racchi M, Watzke HH, High KA, Lively MO. 1993. Human coagulation factor X deficiency caused by a mutant signal peptide that blocks cleavage by signal peptidase but not targeting and translocation to the endoplasmic reticulum. J Biol Chem 265:5735-5740.
    • (1993) J Biol Chem , vol.265 , pp. 5735-5740
    • Racchi, M.1    Watzke, H.H.2    High, K.A.3    Lively, M.O.4
  • 74
    • 0025327383 scopus 로고
    • Reaction of LexA repressor with diisopropyl fluorophosphate. A test of the serine protease model
    • Roland KL, Little JW. 1990. Reaction of LexA repressor with diisopropyl fluorophosphate. A test of the serine protease model. J Biol Chem 265:12828-12835.
    • (1990) J Biol Chem , vol.265 , pp. 12828-12835
    • Roland, K.L.1    Little, J.W.2
  • 75
    • 0026098773 scopus 로고
    • Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast
    • Schneider A, Behrens M, Scherer P, Pratje E, Michaelis G, Schatz G. 1991. Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast. EMBO J 10:247-254.
    • (1991) EMBO J , vol.10 , pp. 247-254
    • Schneider, A.1    Behrens, M.2    Scherer, P.3    Pratje, E.4    Michaelis, G.5    Schatz, G.6
  • 76
    • 0028362616 scopus 로고
    • Purified inner membrane protease I of yeast mitochondria is a heterodimer
    • Schneider A, Oppliger W, Jeno P. 1994. Purified inner membrane protease I of yeast mitochondria is a heterodimer. J Biol Chem 269:8635-8638.
    • (1994) J Biol Chem , vol.269 , pp. 8635-8638
    • Schneider, A.1    Oppliger, W.2    Jeno, P.3
  • 77
    • 0025830411 scopus 로고
    • Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions
    • Shackleton JB, Robinson C. 1991. Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions. J Biol Chem 266:12152-12156.
    • (1991) J Biol Chem , vol.266 , pp. 12152-12156
    • Shackleton, J.B.1    Robinson, C.2
  • 78
    • 0025294104 scopus 로고
    • Two subunits of the canine signal peptidase complex are homologous to yeast SEC11 protein
    • Shelness GS, Blobel G. 1990. Two subunits of the canine signal peptidase complex are homologous to yeast SEC11 protein. J Biol Chem 265:9512-9519.
    • (1990) J Biol Chem , vol.265 , pp. 9512-9519
    • Shelness, G.S.1    Blobel, G.2
  • 79
    • 0023806488 scopus 로고
    • cDNA-derived primary structure of the glycoprotein component of canine microsomal signal peptidase complex
    • Shelness GS, Kanwar YS, Blobel G. 1988. cDNA-derived primary structure of the glycoprotein component of canine microsomal signal peptidase complex. J Biol Chem 265:17063-17070.
    • (1988) J Biol Chem , vol.265 , pp. 17063-17070
    • Shelness, G.S.1    Kanwar, Y.S.2    Blobel, G.3
  • 80
    • 0027401732 scopus 로고
    • Membrane topology and biogenesis of eukaryotic signal peptidase
    • Shelness GS, Lin L, Nicchitta CV. 1993. Membrane topology and biogenesis of eukaryotic signal peptidase. J Biol Chem 265:5201-5208.
    • (1993) J Biol Chem , vol.265 , pp. 5201-5208
    • Shelness, G.S.1    Lin, L.2    Nicchitta, C.V.3
  • 81
    • 0026317885 scopus 로고
    • Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidase
    • Shen LM, Lee JI, Cheng SY, Jutte H, Kuhn A, Dalbey RE. 1991. Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidase. Biochemistry 30:11775-11781.
    • (1991) Biochemistry , vol.30 , pp. 11775-11781
    • Shen, L.M.1    Lee, J.I.2    Cheng, S.Y.3    Jutte, H.4    Kuhn, A.5    Dalbey, R.E.6
  • 82
    • 0028046199 scopus 로고
    • Induction of ethanol dependence increases signal peptidase mRNA levels in rat brain
    • Signs SA, Jacquet R. 1994. Induction of ethanol dependence increases signal peptidase mRNA levels in rat brain. Mol Cell Biochem 159:21-26.
    • (1994) Mol Cell Biochem , vol.159 , pp. 21-26
    • Signs, S.A.1    Jacquet, R.2
  • 83
    • 0026631514 scopus 로고
    • Identification of potential active-site residues in the Escherichia coli leader peptidase
    • Sung M, Dalbey RE. 1992. Identification of potential active-site residues in the Escherichia coli leader peptidase. J Biol Chem 267:13154-13159.
    • (1992) J Biol Chem , vol.267 , pp. 13154-13159
    • Sung, M.1    Dalbey, R.E.2
  • 84
    • 0343326944 scopus 로고
    • mRNA-dependent synthesis of authentic precursor to human placental lactogen: Conversion to its mature hormone form in ascites cell-extracts
    • Szczesna E, Boime I. 1976. mRNA-dependent synthesis of authentic precursor to human placental lactogen: Conversion to its mature hormone form in ascites cell-extracts. Proc Natl Acad Sci USA 75:1179-1183.
    • (1976) Proc Natl Acad Sci USA , vol.75 , pp. 1179-1183
    • Szczesna, E.1    Boime, I.2
  • 86
    • 0028942966 scopus 로고
    • Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: Requirement of detergent or phospholipid for optimal activity
    • Tschantz WR, Paetzel M, Cao G, Suciu D, Inouye M, Dalbey RE. 1995. Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: Requirement of detergent or phospholipid for optimal activity. Biochemistry 54:3935-3941.
    • (1995) Biochemistry , vol.54 , pp. 3935-3941
    • Tschantz, W.R.1    Paetzel, M.2    Cao, G.3    Suciu, D.4    Inouye, M.5    Dalbey, R.E.6
  • 87
    • 0027733662 scopus 로고
    • A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase
    • Tschantz WR, Sung M, Delgado-Partin VM, Dalbey RE. 1993. A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase. J Biol Chem 265:27349-27354.
    • (1993) J Biol Chem , vol.265 , pp. 27349-27354
    • Tschantz, W.R.1    Sung, M.2    Delgado-Partin, V.M.3    Dalbey, R.E.4
  • 88
    • 0026772152 scopus 로고
    • Signal peptidase I of Bacillus subtilis: Patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases
    • van Dijl JM, de Jong A, Vehmaanperä J, Venema G, Bron S. 1992. Signal peptidase I of Bacillus subtilis: Patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases. EMBO J 11:2819-2828.
    • (1992) EMBO J , vol.11 , pp. 2819-2828
    • Van Dijl, J.M.1    De Jong, A.2    Vehmaanperä, J.3    Venema, G.4    Bron, S.5
  • 89
    • 0028966094 scopus 로고
    • Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases
    • van Dijl JM, de Jong A, Venema G, Bron S. 1995. Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases. J Biol Chem 270:3611-3618.
    • (1995) J Biol Chem , vol.270 , pp. 3611-3618
    • Van Dijl, J.M.1    De Jong, A.2    Venema, G.3    Bron, S.4
  • 90
    • 34250096790 scopus 로고
    • Synthesis and processing of Escherichia coli TEM-beta-lactamase and Bacillus licheniformis alpha-amylase in E. coli: The role of signal peptidase I
    • van Dijl JM, Smith H, Bron S, Venema G. 1988. Synthesis and processing of Escherichia coli TEM-beta-lactamase and Bacillus licheniformis alpha-amylase in E. coli: The role of signal peptidase I. Mol Gen Genet 214:55-61.
    • (1988) Mol Gen Genet , vol.214 , pp. 55-61
    • Van Dijl, J.M.1    Smith, H.2    Bron, S.3    Venema, G.4
  • 92
    • 0027443990 scopus 로고
    • In vitro assay for the Bacillus subtilis signal peptidase SipS: Systems for efficient in vitro transcription-translation and processing of precursors of secreted proteins
    • Vehmaanperä J, Gorner A, Venema G, Bron S, van Dijl JM. 1993. In vitro assay for the Bacillus subtilis signal peptidase SipS: Systems for efficient in vitro transcription-translation and processing of precursors of secreted proteins. FEMS Microbiol Lett 114:207-214.
    • (1993) FEMS Microbiol Lett , vol.114 , pp. 207-214
    • Vehmaanperä, J.1    Gorner, A.2    Venema, G.3    Bron, S.4    Van Dijl, J.M.5
  • 93
    • 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 116:17-21.
    • (1983) Eur J Biochem , vol.116 , pp. 17-21
    • Von Heijne, G.1
  • 94
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • von Heijne G. 1985. Signal sequences. The limits of variation. J Mol Biol 154:99-105.
    • (1985) J Mol Biol , vol.154 , pp. 99-105
    • Von Heijne, G.1
  • 95
    • 0011251247 scopus 로고
    • Austin, Texas: R.G. Landes Company
    • von Heijne G. 1994. Signal peptidase. Austin, Texas: R.G. Landes Company.
    • (1994) Signal Peptidase
    • Von Heijne, G.1
  • 96
    • 0020754608 scopus 로고
    • M13 procoat and a preimmunoglobulin share processing specificity but use different membrane receptor mechanisms
    • Watts C, Wickner W, Zimmermann R. 1983. M13 procoat and a preimmunoglobulin share processing specificity but use different membrane receptor mechanisms. Proc Natl Acad Sci USA 50:2809-2813.
    • (1983) Proc Natl Acad Sci USA , vol.50 , pp. 2809-2813
    • Watts, C.1    Wickner, W.2    Zimmermann, R.3
  • 97
    • 0027317361 scopus 로고
    • Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping
    • Whitley P, Nilsson L, von Heijne G. 1993. Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping. Biochemistry 52:8534-8539.
    • (1993) Biochemistry , vol.52 , pp. 8534-8539
    • Whitley, P.1    Nilsson, L.2    Von Heijne, G.3
  • 98
    • 0023393136 scopus 로고
    • Inhibition of purified Escherichia coli leader peptidase by the leader (signal) peptide of bacteriophage M13 procoat
    • Wickner W, Moore K, Dibb N, Geissert D, Rice M. 1987. Inhibition of purified Escherichia coli leader peptidase by the leader (signal) peptide of bacteriophage M13 procoat. J Bacteriol 169:3821-3822.
    • (1987) J Bacteriol , vol.169 , pp. 3821-3822
    • Wickner, W.1    Moore, K.2    Dibb, N.3    Geissert, D.4    Rice, M.5
  • 99
    • 0020322859 scopus 로고
    • The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme
    • Wolfe PB, Silver P, Wickner W. 1982. The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme. J Biol Chem 257:7898-7902.
    • (1982) J Biol Chem , vol.257 , pp. 7898-7902
    • Wolfe, P.B.1    Silver, P.2    Wickner, W.3
  • 100
    • 0021100176 scopus 로고
    • Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope
    • Wolfe PB, Wickner W, Goodman JM. 1983. Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J Biol Chem 255:12073-12080.
    • (1983) J Biol Chem , vol.255 , pp. 12073-12080
    • Wolfe, P.B.1    Wickner, W.2    Goodman, J.M.3
  • 101
    • 0024508339 scopus 로고
    • Solubilization and characterization of yeast signal peptidase
    • YaDeau JT, Blobel G. 1989. Solubilization and characterization of yeast signal peptidase. J Biol Chem 264:2928-2934.
    • (1989) J Biol Chem , vol.264 , pp. 2928-2934
    • Yadeau, J.T.1    Blobel, G.2
  • 102
    • 0026011095 scopus 로고
    • Yeast signal peptidase contains a glycoprotein and the See11 gene product
    • YaDeau JT, Klein C, Blobel G. 1991. Yeast signal peptidase contains a glycoprotein and the See11 gene product. Proc Natl Acad Sci USA 55:517-521.
    • (1991) Proc Natl Acad Sci USA , vol.55 , pp. 517-521
    • Yadeau, J.T.1    Klein, C.2    Blobel, G.3
  • 103
    • 0019410055 scopus 로고
    • Leader peptidase is found in both the inner and outer membranes of Escherichia coli
    • Zwizinski C, Date T, Wickner W. 1981. Leader peptidase is found in both the inner and outer membranes of Escherichia coli. J Biol Chem 256:3593-3597.
    • (1981) J Biol Chem , vol.256 , pp. 3593-3597
    • Zwizinski, C.1    Date, T.2    Wickner, W.3
  • 104
    • 0019129862 scopus 로고
    • Purification and characterization of leader (signal) peptidase from Escherichia coli
    • Zwizinski C, Wickner W. 1980. Purification and characterization of leader (signal) peptidase from Escherichia coli. J Biol Chem 255:7973-7977.
    • (1980) J Biol Chem , vol.255 , pp. 7973-7977
    • Zwizinski, C.1    Wickner, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.