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Volumn 12, Issue 15, 1998, Pages 2318-2331

Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: Identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases

Author keywords

Bacillus subtilis; Leader peptidase; Paralogous gene family; Protein secretion; Signal peptidase

Indexed keywords

ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; MULTIGENE FAMILY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN SECRETION; TEMPERATURE SENSITIVE MUTANT;

EID: 0032146073     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.15.2318     Document Type: Article
Times cited : (145)

References (52)
  • 2
    • 0025769806 scopus 로고
    • Mitochondrial inner membrane protease 1 of Saccharomyces cerevisiae shows sequence similarity to the Escherichia coli leader peptidase
    • Behrens, M., G. Michaelis, and E. Pratje. 1991. Mitochondrial inner membrane protease 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
  • 3
    • 0027291327 scopus 로고
    • Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad
    • Black, M.T. 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
  • 5
    • 0029809574 scopus 로고    scopus 로고
    • Bacillus subtilis can modulate its capacity and specificity for protein secretion by temporally expression of the sipS gene for signal peptidase I
    • Bolhuis, A., A. Sorokin, V. Azevedo, S.D. Ehrlich, P.G. Braun, A. de Jong, G. Venema, S. Bron, and J.M. van Dijl. 1996. Bacillus subtilis can modulate its capacity and specificity for protein secretion by temporally expression of the sipS gene for signal peptidase I. Mol. Miciobiol. 22: 605-618.
    • (1996) Mol. Miciobiol. , 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
  • 6
    • 0015335342 scopus 로고
    • Ultraviolet inactivation and excision repair in Bacillus subtilis. Construction and characterization of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives
    • Bron, S. and G. Venema. 1972. Ultraviolet inactivation and excision repair in Bacillus subtilis. Construction and characterization of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives. Mutat. Res. 15: 1-10.
    • (1972) Mutat. Res. , vol.15 , pp. 1-10
    • Bron, S.1    Venema, G.2
  • 7
    • 0023894180 scopus 로고
    • Sec11 is required for signal peptide processing and yeast cell growth
    • Böhni, P.C., R.J. Deshaies, and R.W. Schekman. 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
  • 9
    • 0029796449 scopus 로고    scopus 로고
    • Molecular cloning and expression of the spsB gene encoding an essential type I signal peptidase from Staphylococcus aureus
    • Cregg, K.M., E.I. Wilding, and M.T. Black. 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
  • 10
    • 0025293361 scopus 로고
    • Biotination of proteins in vivo
    • Cronan, J.E. 1990. Biotination of proteins in vivo. J. Biol. Chem. 265: 10327-10333.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10327-10333
    • Cronan, J.E.1
  • 11
    • 0022400507 scopus 로고
    • Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane
    • Dalbey, R.E. and W. Wickner. 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
  • 12
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes: A new protease family
    • Dalbey, R.E. and G. von Heijne. 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
  • 13
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • Dalbey, R.E., M.O. Lively, S. Bron, and J.M. van Dijl. 1997. The chemistry and enzymology of the type I signal peptidases. Protein Sci. 6: 1129-1138.
    • (1997) Protein Sci. , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    Van Dijl, J.M.4
  • 14
    • 0030927703 scopus 로고    scopus 로고
    • In addition to SEC11, a newly identified gene, SPC3, is essential for signal peptidase activity in the yeast endoplasmic reticulum
    • Fang, H., C. Mullins, and N. Green. 1997. In addition to SEC11, a newly identified gene, SPC3, is essential for signal peptidase activity in the yeast endoplasmic reticulum. J. Biol. Chem. 272: 13152-13158.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13152-13158
    • Fang, H.1    Mullins, C.2    Green, N.3
  • 15
  • 18
    • 0024428204 scopus 로고
    • A subunit of mammalian signal pepsidase is homologous to yeast SEC11 protein
    • Greenburg, G. G.S. Shelness, and G. Blobel. 1989. A subunit of mammalian signal pepsidase 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
  • 19
    • 0028886749 scopus 로고
    • Bacillus amyloliquefaciens possesses a second type I signal peptidase with extensive sequence similarity to other Bacillus SPases
    • Hoang, V. and J. Hofemeister. 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
  • 20
    • 0028817078 scopus 로고
    • Expression of the subtilisin Carlsberg-encoding gene in Bacillus licheniformis and Bacillus subtilis
    • Jacobs, M.F. 1995. Expression of the subtilisin Carlsberg-encoding gene in Bacillus licheniformis and Bacillus subtilis. Gene 152: 69-74.
    • (1995) Gene , vol.152 , pp. 69-74
    • Jacobs, M.F.1
  • 21
    • 0030014628 scopus 로고    scopus 로고
    • Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion
    • Jander, G., J.E. Cronan, and J. Beckwith. 1996. Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion. J. Bacteriol 178: 3049-3058.
    • (1996) J. Bacteriol , vol.178 , pp. 3049-3058
    • Jander, G.1    Cronan, J.E.2    Beckwith, J.3
  • 22
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko, T., S. Sato, H. Kotani, A. Tanaka, E. Asamizu, Y. Nakamura, N. Miyajima, M. Hirosawa, M. Sugiura, S. Sasamoto et al. 1996. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 30: 109-136.
    • (1996) DNA Res. , vol.30 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6    Miyajima, N.7    Hirosawa, M.8    Sugiura, M.9    Sasamoto, S.10
  • 23
    • 0030605248 scopus 로고    scopus 로고
    • A xylose-inducible Bacillus subtilis integration vector and its application
    • Kim, L., A. Mogk, and W. Schumann. 1996. A xylose-inducible Bacillus subtilis integration vector and its application. Gene 181: 71-76.
    • (1996) Gene , vol.181 , pp. 71-76
    • Kim, L.1    Mogk, A.2    Schumann, W.3
  • 25
    • 0024064875 scopus 로고
    • Mutants of B. subtilis defective in protein export
    • Kontinen, V.P. and M. Sarvas. 1988. Mutants of B. subtilis defective in protein export. J. Gen. Microbiol. 134: 2333-2344.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2333-2344
    • Kontinen, V.P.1    Sarvas, M.2
  • 27
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen, J. 1984. Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 10: 203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 28
    • 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, W.J.J., A. de Jong, G.B.A. Wisman, H. Tjalsma, G. Venema, S. Bron, and J.M. van Dijl. 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
  • 29
    • 0030914529 scopus 로고    scopus 로고
    • The yeast SPC22/23 homologue Spc3p is essential for signal peptidase activity
    • Meyer, H.A. and E. Hartmann. 1997. The yeast SPC22/23 homologue Spc3p is essential for signal peptidase activity. J. Biol. Chem. 272: 13159-13164.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13159-13164
    • Meyer, H.A.1    Hartmann, E.2
  • 30
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J.H. 1982. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1982) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 31
    • 0002241511 scopus 로고
    • (ed. A.L. Sonenshein, J.A. Hoch, and R. Losick), American Society for Microbiology, Washington, D.C.
    • Msadek, T., F. Kunst, and G. Rapoport. 1993. In Bacillus subtilis and other Gram-positive bacteria (ed. A.L. Sonenshein, J.A. Hoch, and R. Losick), pp. 729-745. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 729-745
    • Msadek, T.1    Kunst, F.2    Rapoport, G.3
  • 32
    • 0026583534 scopus 로고
    • Molecular cloning of a cDNA encoding the glycoprotein of hen oviduct microsomal signal peptidase
    • Newsome, A.L., J.W. McLean, and M.O. Lively. 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
  • 33
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari, J., T.D. Fox, and P. Walter. 1993. A mitochondrial protease with two catalytic 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
  • 34
    • 0020438726 scopus 로고
    • Molecular cloning of α-amylase gene from Bacillus amyloliquefadens and its expression in Bacillus subtilis
    • Palva, I. 1982. Molecular cloning of α-amylase gene from Bacillus amyloliquefadens and its expression in Bacillus subtilis. Gene 19:81-87.
    • (1982) Gene , vol.19 , pp. 81-87
    • Palva, I.1
  • 35
    • 0031033450 scopus 로고    scopus 로고
    • Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase
    • Paetzel, M. and R.E. Dalbey. 1997. Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase. Trends. Biochem. Sci. 22:28-31.
    • (1997) Trends. Biochem. Sci. , vol.22 , pp. 28-31
    • Paetzel, M.1    Dalbey, R.E.2
  • 38
    • 0025294104 scopus 로고
    • Two subunits of the canine signal peptidase complex are homologous to yeast Sec11 protein
    • Shelness, G.S. and G. Blobel. 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
  • 39
    • 0028046199 scopus 로고
    • Induction of ethanol dependence increases signal peptidase mRNA levels in rat brain
    • Signs, S.A. and R. Jacquet. 1994. Induction of ethanol dependence increases signal peptidase mRNA levels in rat brain. Mol. Cell. Biochem. 139: 21-26.
    • (1994) Mol. Cell. Biochem. , vol.139 , pp. 21-26
    • Signs, S.A.1    Jacquet, R.2
  • 40
    • 0027264995 scopus 로고
    • Predicting the topology of eukaryotic membrane proteins
    • Sipos, L. and G. von Heijne. 1993. Predicting the topology of eukaryotic membrane proteins. Eur. J. Biochem. 213: 1333-1340.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1333-1340
    • Sipos, L.1    Von Heijne, G.2
  • 42
    • 0030868265 scopus 로고    scopus 로고
    • Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities: Constitutive and temporally controlled expression of different sip genes
    • Tjalsma, H., M.A. Noback, S. Bron, G. Venema, K. Yamane, and J.M. van Dijl. 1997. Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities: Constitutive and temporally controlled expression of different sip genes. J. Biol. Chem. 272: 25983-25992.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25983-25992
    • Tjalsma, H.1    Noback, M.A.2    Bron, S.3    Venema, G.4    Yamane, K.5    Van Dijl, J.M.6
  • 44
    • 0027733662 scopus 로고
    • A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase
    • Tschantz, W.R., M. Sung, V.M. Delgado-Partin, and R.E. Dalbey. 1993. A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase. J. Biol. Chem. 268: 27349-27354.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27349-27354
    • Tschantz, W.R.1    Sung, M.2    Delgado-Partin, V.M.3    Dalbey, R.E.4
  • 45
    • 34250096790 scopus 로고
    • Synthesis and processing of Escherichia coli TEM-β-lactamase and Bacillus licheniformis α-amylase in Escherichia coli: The role of signal peptidase I
    • van Dijl, J.M., A. de Jong, H. Smith, S. Bron, and G. Venema. 1988. Synthesis and processing of Escherichia coli TEM-β-lactamase and Bacillus licheniformis α-amylase in Escherichia 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    De Jong, A.2    Smith, H.3    Bron, S.4    Venema, G.5
  • 46
    • 0025869932 scopus 로고
    • Signal peptidase I overproduction results in increased efficiencies of export and maturation of hybrid secretory proteins in Escherichia coli
    • van Dijl, J.M., A. de Jong, H. Smith, S. Bron, and G. Venema. 1991a. Signal peptidase I overproduction results in increased efficiencies of export and maturation of hybrid secretory proteins in Escherichia coli. Mol. & Gen. Genet. 227: 40-48.
    • (1991) Mol. & Gen. Genet. , vol.227 , pp. 40-48
    • Van Dijl, J.M.1    De Jong, A.2    Smith, H.3    Bron, S.4    Venema, G.5
  • 47
    • 0025836134 scopus 로고
    • Non-functional expression of Escherichia coli signal peptidase I in Bacillus subtilis
    • _. 1991b. Non-functional expression of Escherichia coli signal peptidase I in Bacillus subtilis. J. Gen. Microbiol. 137: 2073-2083.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2073-2083
  • 48
    • 0026772152 scopus 로고
    • Signal peptidase I of Bacillus subtilis: Patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases
    • van Dijl, J.M., A. de Jong, J. Vehmaanperá, G. Venema, and S. Bron. 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    Vehmaanperá, J.3    Venema, G.4    Bron, S.5
  • 49
    • 0028966094 scopus 로고
    • Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis
    • van Dijl, J.M., A. de Jong, G. Venema, and S. Bron. 1995. Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. 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
  • 50
    • 0025615652 scopus 로고
    • Isolation and characterisation of comL, a transcriptional unit involved in competence development of Bacillus subtilis
    • van Sinderen, D., S. Withoff, H. Boels, and G. Venema. 1990. Isolation and characterisation of comL, a transcriptional unit involved in competence development of Bacillus subtilis. Mol. & Gen. Genet. 224: 396-404.
    • (1990) Mol. & Gen. Genet. , vol.224 , pp. 396-404
    • Van Sinderen, D.1    Withoff, S.2    Boels, H.3    Venema, G.4
  • 51
    • 0025809486 scopus 로고
    • New pUC-derived cloning vectors with different selectable markers and DNA replication origins
    • Vieria, J. and J. Messing. 1990. New pUC-derived cloning vectors with different selectable markers and DNA replication origins. Gene 100: 189-194.
    • (1990) Gene , vol.100 , pp. 189-194
    • Vieria, J.1    Messing, J.2
  • 52
    • 0022917641 scopus 로고
    • Host/vector interactions which affect the viability of recombinant phage lambda clones
    • Wertman, K.F., A.R. Wyman, and D. Botstein. 1986. Host/vector interactions which affect the viability of recombinant phage lambda clones. Gene 49: 253-262.
    • (1986) Gene , vol.49 , pp. 253-262
    • Wertman, K.F.1    Wyman, A.R.2    Botstein, D.3


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