Skip to main content
SpringerLink
Log in

Signal Peptidases

  • Conference paper
Protein Secretion and Export in Bacteria

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 125))

Abstract

This review will attempt to summarize the current literature concerned with the in vitro processing of precursor proteins by solubilized signal peptidases; by necessity, it will mainly be concerned with the bacterial signal peptidases. A number of recent reviews concerned with various aspects of protein export have been published (Benson et al. 1985; Bankaitis et al. 1985; Randall and Hardy 1984; Silhavy et al. 1983) and these topics will not be discussed, except in the context that they pertain to the signal peptidases.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Austen BM, Hermon-Taylor J, Kaderbhai MA, Ridd DH (1984) Design and synthesis of a consensus signal sequence that inhibits protein translocation into rough microsomal vesicles. Biochem J 224: 317–325

    PubMed  CAS  Google Scholar 

  • Bankaitis VA, Bassford PJ Jr (1985) Proper interaction between at least two components is required for efficient export of proteins to the Escherichia coli cell envelope. J Bacteriol 161: 169–178

    PubMed  CAS  Google Scholar 

  • Bankaitis VA, Rasmussen BA, Bassford PJ Jr (1984) Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide. Cell 37: 243–252

    PubMed  CAS  Google Scholar 

  • Bankaitis VA, Ryan JP, Rasmussen BA, Bassford PJ Jr (1985) The use of genetic techniques to analyze protein export in Escherichia coli. In: Knauf PA, Cook JS (eds) Current topics in membranes and transport, vol 24. Academic Press Orlando, Florida, pp 105–150

    Google Scholar 

  • Bassford P, Beckwith J (1979) Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm. Nature 277: 538–541

    PubMed  CAS  Google Scholar 

  • Bassford PJ Jr, Silhavy TJ, Beckwith JR (1979) Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm. J Bacteriol 139: 19–31

    PubMed  CAS  Google Scholar 

  • Bassford PJ Jr, Bankaitis VA, Rasmussen BA, Ryan JP (1984) Genetic studies on the mechanism of secretion of maltose-binding protein of E. coli. J Cell Biochem 24: 303–309

    Google Scholar 

  • 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

    PubMed  CAS  Google Scholar 

  • Benson SA, Hall MN, Silhavy TJ (1985) Genetic analysis of protein export in Escherichia coli K-12. Ann Rev Biochem 54: 101–134

    PubMed  CAS  Google Scholar 

  • Blobel G, Dobberstein B (1975) Transfer of proteins across membranes. J Cell Biol 67: 835–851

    PubMed  CAS  Google Scholar 

  • Bohni PC, Daum G, Schatz G (1983) Import of proteins into mitochondria. J Biol Chem 258: 4937–4943

    PubMed  CAS  Google Scholar 

  • Casadaban MJ (1976) Transposition and fusion of the lac operon to selected promoters in E. coli using bacteriophage lambda and Mu. J Mol Biol 104: 541–555

    PubMed  CAS  Google Scholar 

  • Chen L, Rhoads D, Tai PC (1985) Alkaline phosphatase and OmpA protein can be translocated posttranslationally into membrane vesicles of Escherichia coli. J Bacteriol 161: 973–980

    PubMed  CAS  Google Scholar 

  • Chung HC, Goldberg AL (1983) Purification and characterization of protease So, a cytoplasmic serine protease in Escherichia coli. J Bacteriol 154: 231–238

    PubMed  CAS  Google Scholar 

  • Dalbey RE, Wickner W (1985) Leader peptidase is required for the release of exported proteins from the outer surface of the Escherichia coli plasma membrane. J Biol Chem 260: 15925–15931

    PubMed  CAS  Google Scholar 

  • Daniels CJ, Bole DG, Quay SC, Oxender DL (1981) Role of membrane potential in the secretion of protein into the periplasm of Escherichia coli. Proc Natl Acad Sci USA 78: 5396–5400

    PubMed  CAS  Google Scholar 

  • Date T (1983) Demonstration by a novel genetic technique that leader peptidase is an essential enzyme of Escherichia coli. J Bacteriol 154: 76–83

    PubMed  CAS  Google Scholar 

  • 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

    PubMed  CAS  Google Scholar 

  • Dev IK, Ray PH (1984) Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B. J Biol Chem 259: 11114–11120

    PubMed  CAS  Google Scholar 

  • Dev IK, Harvey RJ, Ray PH (1985) Inhibition of prolipoprotein signal peptidase by globomycin. J Biol Chem 260: 5891–5894

    PubMed  CAS  Google Scholar 

  • Dev IK, Harvey RJ, Ray PH (1986) Identification of the oligopeptidase as the major cytoplasmic signal peptide hydrolase in Salmonella typhimurium. Unpublished data

    Google Scholar 

  • Emr SD, Bassford PJ (1982) Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. J Biol Chem 257: 5852–5860

    PubMed  CAS  Google Scholar 

  • Emr SD, Silhavy TJ (1980) Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor. J Mol Biol 141: 63–90

    PubMed  CAS  Google Scholar 

  • Emr SD, Silhavy TJ (1982) Molecular components of the signal sequence that function in the initiation of protein export. J Cell Biol 95: 689–696

    PubMed  CAS  Google Scholar 

  • Ferenci T, Klotz U (1978) Affinity chromatographic isolation of the periplasmic maltose binding protein of Escherichia coli. FEBS 94: 213–217

    CAS  Google Scholar 

  • Ferenci T, Randall LL (1979) Precursor maltose-binding protein is active in binding substrate. J Biol Chem 254: 9979–9981

    PubMed  CAS  Google Scholar 

  • Fujimoto Y, Watanabe Y, Uchida M, Ozaki M (1984) Mammalian signal peptidase: partial purification and general characterization of the signal peptidase from microsomal membranes of porcine pancreas. J Biochem 96: 1125–1131

    PubMed  CAS  Google Scholar 

  • Goodman JM, Watts C, Wickner W (1981) Membrane assembly: posttranslational insertion of M13 procoat protein into E. coli membranes and its proteolytic conversion to coat protein in vitro. Cell 24: 437–441

    PubMed  CAS  Google Scholar 

  • Habener JF, Rosenblatt M, Dee PC, Potts JT Jr (1979) Cellular processing of pre-proparathyroid hormone involves rapid hydrolysis of the leader sequence. J Biol Chem 254: 10596–10599

    PubMed  CAS  Google Scholar 

  • Halegoua S, Inouye M (1979) Translocation and assembly of outer membrane proteins of Escherichia coli. Selective accumulation of precursors and novel assembly of intermediates caused by phenethyl alcohol. J Mol Biol 130: 39–61

    PubMed  CAS  Google Scholar 

  • Hussain M, Ichihara S, Mizushima S (1980) Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. J Biol Chem 255: 3707–3712

    PubMed  CAS  Google Scholar 

  • Hussain M, Ichihara S, Mizushima S (1982a) Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane. J Biol Chem 257: 5177–5182

    PubMed  CAS  Google Scholar 

  • Hussain M, Ozawa Y, Ichihara S, Mizushima S (1982 b) Signal peptide digestion in Escherichia coli. Eur J Biochem 129: 233–239

    Google Scholar 

  • Ichihara S, Hussain M, Mizushima S (1981) Characterization of new membrane lipoproteins and their precursors of Escherichia coli. J Biol Chem 256: 3125–3129

    PubMed  CAS  Google Scholar 

  • Ichihara S, Hussain M, Mizushima S (1982) Mechanism of export of outer membrane lipoproteins through the cytoplasmic membrane in Escherichia coli. J Biol Chem 257: 495–500

    PubMed  CAS  Google Scholar 

  • Ichihara S, Beppu N, Mizushima S (1984) Protease IV, a cytoplasmic membrane protein of Escherichia coli, has signal peptide peptidase activity. J Biol Chem 259: 9853–9857

    PubMed  CAS  Google Scholar 

  • Innis MA, Tokunaga M, Williams ME, Loranger JM, Chang SY, Chang S, Wu HC (1984) Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene. Proc Natl Acad Sci USA 81: 3708–3712

    PubMed  CAS  Google Scholar 

  • Inouye H, Beckwith J (1977) Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro. Proc Natl Acad Sci USA 74: 1440–1444

    PubMed  CAS  Google Scholar 

  • Inouye S, Wang SS, Sekizawa J, Halegoua S, Inouye M (1977) Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane. Proc Natl Acad Sci USA 74: 1004–1008

    PubMed  CAS  Google Scholar 

  • Inouye S, Soberson X, Franceschini T, Nakamura K, Itakura K, Inouye M (1982) Role of positive charge on the amino-terminal region of the signal peptide in protein secretion across the membrane. Proc Natl Acad Sci USA 79: 3438–3441

    PubMed  CAS  Google Scholar 

  • Inouye S, Vlasuk GP, Hsiung H, Inouye M (1984) Effects of mutations at glycine residues in the hydrophobic region of the Escherichia coli prolipoprotein signal peptide on the secretion across the membrane. J Biol Chem 259: 3729–3733

    PubMed  CAS  Google Scholar 

  • Inukai M, Inouye M (1983) Association of the prolipoprotein accumulated in the presence of globomycin with the outer membrane of Escherichia coli. Eur J Biochem 130: 27–32

    PubMed  CAS  Google Scholar 

  • Inukai M, Takeuchi M, Shimizu K, Arai M (1978) Mechanism of action of globomycin. J Antibiot 31: 1203–1205

    PubMed  CAS  Google Scholar 

  • Ito K (1982) Purification of the precursor form of maltose-binding protein, a periplasmic protein of Escherichia coli. J. Biol Chem 257: 9895–9897

    PubMed  CAS  Google Scholar 

  • Ito K, Bassford PJ Jr, Beckwith J (1981) Protein localization in E. coli: is there a common step in the secretion of periplasmic and outer-membrane proteins? Cell 24: 707–717

    PubMed  CAS  Google Scholar 

  • Jackson RC (1983) Quantiative assay for signal peptidase. Meth Enzymol 96: 784–794

    PubMed  CAS  Google Scholar 

  • Jackson RC, Blobel G (1977) Post-translational cleavage of presecretory proteins with an extract of rough microsomes from dog pancreas containing signal peptidase activity. Proc Natl Acad Sci USA 74: 5598–5602

    PubMed  CAS  Google Scholar 

  • Jackson RC, Blobel G (1980) Post-translational processing of full-length presecretory proteins with canine pancreatic signal peptidase. Annals New York Acad Sci 343: 391–404

    CAS  Google Scholar 

  • 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

    PubMed  CAS  Google Scholar 

  • Kamio Y, Lin CK, Regue M, Wu HC (1985) Characterization of the ileS-lsp operon in Escherichia coli. J Biol Chem 260: 5616–5620

    PubMed  CAS  Google Scholar 

  • Koren R, Burstein Y, Soreq H (1983) Synthetic leader peptide modulates secretion of proteins from microinjected Xenopus oocytes. Proc Natl Acad Sci USA 80: 7205–7209

    PubMed  CAS  Google Scholar 

  • Koshland D, Sauer RT, Botstein D (1982) Diverse effects of mutations in the signal sequence on the secretion of ß-lactamase in Salmonella typhimurium. Cell 30: 903–914

    PubMed  CAS  Google Scholar 

  • Kumamoto CA, Oliver DB, Beckwith J (1984) Signal sequence mutations disrupt feedback between secretion of an exported protein and its synthesis in E. coli. Nature 308: 863–864

    CAS  Google Scholar 

  • Lazdunski C, Baty D, Pages JM (1979) Procaine, a local anesthetic interacting with the cell membrane, inhibits the processing of precursor forms of periplasmic proteins in Escherichia coli. Eur J Biochem 96: 49–57

    PubMed  CAS  Google Scholar 

  • Lin JJC, Kanazawa H, Ozols J, Wu HC (1978) An Escherichia coli mutant with an amino acid alteration within the signal sequence of outer membrane prolipoprotein. Proc Natl Acad Sci USA 75: 4891–4895

    PubMed  CAS  Google Scholar 

  • Lin JJC, Kanazawa H, Wu HC (1980a) Assembly of outer membrane lipoprotein in an Escherichia coli mutant with a single amino acid replacement within the signal sequence of prolipoprotein. J Bacteriol 141: 550–557

    PubMed  CAS  Google Scholar 

  • Lin JJC, Kanazawa H, Wu HC (1980b) Purification and characterization of the outer membrane lipoprotein from an Escherichia coli mutant altered in the signal sequence of prolipoprotein. J Biol Chem 255: 1160–1163

    PubMed  CAS  Google Scholar 

  • Lively MO, Walsh KA (1983) Hen oviduct signal peptidase is an integral membrane protein. J Biol Chem 258: 9488–9495

    PubMed  CAS  Google Scholar 

  • Marchal C, Perrin D, Hedgpeth J, Hofnung M (1980) Synthesis and maturation of lambda receptor in Escherichia coli K-12: in vivo and in vitro expression of gene lamB under lac promoter control. Proc Natl Acad Sci USA 77: 1491–1495

    PubMed  CAS  Google Scholar 

  • McAda PC, Douglas MG (1982) A neutral metallo-endoprotease involved in the processing of an F1-ATPase subunit precursor in mitochondria. J Biol Chem 257: 3177–3182

    PubMed  CAS  Google Scholar 

  • Michaelis S, Beckwith J (1982) Mechanism of incorporation of cell envelope proteins in Escherichia coli. Ann Rev Microbiol 36: 435–464

    CAS  Google Scholar 

  • Minkley EG Jr (1984) Purification and characterization of pro-TraTp, the signal sequence containing precursor of a secreted protein encoded by the sex factor. J Bacteriol 138: 464–473

    Google Scholar 

  • Mollay C, Vilas U, Kreil G (1982) Cleavage of honeybee prepromelittin by an endoprotease from rat liver microsomes: identification of intact signal peptide. Proc Natl Acad Sci USA 79: 2260–2263

    PubMed  CAS  Google Scholar 

  • Novak P, Ray PH, Dev IK (1985) Localization and purification of two signal peptide hydrolases from Escherichia coli. J Biol Chem 261: 420–427

    Google Scholar 

  • Omoto S, Ogino H, Inouye S (1981) Studies on SF-1902 A2-A5, minor components of SF-1902 (Globomycin). J Antibiot 34: 1416–1423

    PubMed  CAS  Google Scholar 

  • Pacaud M (1982) Purification and characterization of two novel proteolytic enzymes in membranes of Escherichia coli. J Biol Chem 257: 4333–339

    PubMed  CAS  Google Scholar 

  • Perlman D, Halvorson HO (1983) A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol 167: 391–409

    PubMed  CAS  Google Scholar 

  • Pugsley AP, Schwartz M (1985) Export and secretion of proteins by bacteria. FEMS Microbiol Rev 32: 1–36

    Google Scholar 

  • Randall LL, Hardy SJS (1984) Export of protein in bacteria. Microbiol Rev 48: 290–298

    PubMed  CAS  Google Scholar 

  • Ray PH, Dev IK, Miller TA, Bassford PJ Jr (1986) Evidence for another signal peptidase: In vitro processing of maltose-binding protein precursors having alterations in their signal sequences. Submitted for publication

    Google Scholar 

  • Regue M, Remenick J, Tokunaga M, Mackie GA, Wu HC (1984) Mapping of the lipoprotein signal peptidase gene (lsp). J Bacteriol 158: 632–635

    PubMed  CAS  Google Scholar 

  • Roggenkamp R, Kunstermann-Kuhn B, Hollenberg CP (1981) Expression and processing of bacterial ß-lactamase in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci USA 78: 4466–4470

    PubMed  CAS  Google Scholar 

  • Roggenkamp R, Hoppe J, Hollenberg CP (1983) Specific processing of the bacterial ß-lactamase precursor in Saccharomyces cerevisiae. J Cell Biochem 22: 141–149

    PubMed  CAS  Google Scholar 

  • Roggenkamp R, Dargatz H, Hollenberg CP (1985) Precursor of ß-lactamase is enzymatically inactive. J Biol Chem 260: 1508–1512

    PubMed  CAS  Google Scholar 

  • Shapiro AL, Vinuela E, Maizel JV Jr (1967) Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Comm 28: 815–820

    PubMed  CAS  Google Scholar 

  • Silhavy TJ, Shuman HA, Beckwith J, Schwartz M (1977) Use of gene fusions to study outer membrane protein localization in Escherichia coli. Proc Natl Acad Sci USA 74: 5411–5415

    PubMed  CAS  Google Scholar 

  • Silhavy TJ, Bassford PJ Jr, Beckwith JR (1979) A genetic approach to the study of protein localization in Escherichia coli. In: Inouye M (ed) Bacterial outer membranes: biogenesis and functions. Wiley, New York, pp 203–254

    Google Scholar 

  • Silhavy TJ, Benson SA, Emr SD (1983) Mechanisms of protein localization. Microbiol Rev 47: 313–344

    PubMed  CAS  Google Scholar 

  • Silver P, Wickner W (1983) Genetic mapping of the Escherichia coli leader (signal) peptidase gene (lep): a new approach for determining the map position of a cloned gene. J Bacteriol 154: 569–572

    PubMed  CAS  Google Scholar 

  • Silver P, Watts C, Wickner W (1981) Membrane assembly from purified components. I. Isolated M13 procoat does not require ribosomes or soluble proteins for processing by membranes. Cell 25: 341–345

    PubMed  CAS  Google Scholar 

  • Stern JB, Jackson RC (1985) Peptide products of the cleavage of bovine preprolactin by signal peptidase. Arch Biochem Biophys 237: 244–252

    PubMed  CAS  Google Scholar 

  • Strauss AW, Zimmerman M, Boime I, Ashe B, Mumford RA, Alberts AW (1979) Characterization of an endopeptidase involved in pre-protein processing. Proc Natl Acad Sci USA 76: 4225–4229

    PubMed  CAS  Google Scholar 

  • Strauss AW, Zimmerman M, Mumford RA, Alberts AW (1980) Processing of pre-proalbumin and pre-placental lactogen. Ann New York Acad Sci 343: 168–191

    CAS  Google Scholar 

  • Talmadge K, Stahl S, Gilbert W (1980) Eukaryotic signal sequence transports insulin antigen in Escherichia coli. Proc Natl Acad Sci USA 77: 3369–3373

    PubMed  CAS  Google Scholar 

  • Tokunaga H, Wu HC (1984) Studies on the modification and processing of prolipoprotein in Escherichia coli. J Biol Chem 259: 6098–6104

    PubMed  CAS  Google Scholar 

  • Tokunaga M, Loranger JM, Wolfe PB, Wu HC (1982a) Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase. J Biol Chem 257: 9922–9925

    PubMed  CAS  Google Scholar 

  • Tokunaga M, Tokunaga H, Wu HC (1982 b) Post-translational modification and processing of Escherichia coli prolipoprotein in vitro. Proc Natl Acad Sci USA 79: 2255–2259

    Google Scholar 

  • Tokunaga M, Loranger JM, Wu HC (1983) Prolipoprotein modification and processing enzymes in Escherichia coli. J Biol Chem 259: 3825–3830

    Google Scholar 

  • Tokunaga M, Loranger JM, Wu HC (1984) A distinct signal peptidase for prolipoprotein in Escherichia coli. J Cell Biochem 24: 113–120

    PubMed  CAS  Google Scholar 

  • Tokunaga M, Loranger JM, Chang S-Y, Regue M, Chang S, Wu HC (1985) Identification of prolipoprotein signal peptidase and genomic organization of the lsp gene in Eschericia coli. J Biol Chem 260: 5610–5615

    PubMed  CAS  Google Scholar 

  • Vimr ER, Green L, Miller CG (1983) Oligopeptidase-deficient mutants of Salmonella typhimurium. J Bacteriol 153: 1259–1265

    PubMed  CAS  Google Scholar 

  • Vlasuk GP, Inouye S, Ito H, Itakura K, Inouye M (1983) Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli. J Biol Chem 258: 7141–7148

    PubMed  CAS  Google Scholar 

  • Vlasuk GP, Inouye S, Inouye M (1984) Effects of replacing serine and threonine residues within the signal peptide on the secretion of the major outer membrane lipoprotein of Escherichia coli. J Biol Chem 259: 6195–6200

    PubMed  CAS  Google Scholar 

  • von Heijne G (1984) How signal sequences maintain cleavage specificity. J Mol Biol 173: 243–251

    Google Scholar 

  • Watson MEE (1984) Compilation of published signal sequences. Nucleic Acids Research 12: 5145–5164

    PubMed  CAS  Google Scholar 

  • Watts C, Wickner W, Zimmermann R (1983) M13 procoat and a pre-immunoglobulin share processing specificity but use different membrane receptor mechanisms. Proc Natl Acad Sci USA 80: 2809–2813

    PubMed  CAS  Google Scholar 

  • Wickner W, Mandel G, Zwizinski C, Bates M, Killick T (1978) Synthesis of phage M13 coat protein and its assembly into membranes in vitro. Proc Natl Acad Sci USA 75: 1754–1758

    PubMed  CAS  Google Scholar 

  • 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

    PubMed  CAS  Google Scholar 

  • Wolfe PB, Wickner W, Goodman JM (1983 a) Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J Biol Chem 258: 12073–12080

    Google Scholar 

  • Wolfe PB, Zwizinski C, Wickner W (1983 b) Purification and characterization of leader peptidase from Escherichia coli. Methods Enzymol 97: 40–46

    Google Scholar 

  • Wolfe PR, Rice M, Wickner W (1985) Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli. J Biol Chem 260: 1836–1841

    PubMed  CAS  Google Scholar 

  • Yamagata H, Daishima K, Mizushima S (1983a) Cloning and expression of a gene coding for the prolipoprotein signal peptidase of Escherichia coli. FEBS Lett 158: 301–303

    PubMed  CAS  Google Scholar 

  • Yamagata H, Taguchi N, Daishima K, Mizushima S (1983b) Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coli. MGG 192: 10–14

    PubMed  CAS  Google Scholar 

  • Yu F, Yamada H, Daishima K, Mizushima S (1984) Nucleotide sequence of the Isp A gene, the structural gene for lipoprotein signal peptidase of Escherichia coli. FEBS Lett 173: 264–268

    PubMed  CAS  Google Scholar 

  • Zwizinski C, Wickner W (1980) Puficiation and characterization of leader (signal) peptidase from Escherichia coli. J Biol Chem 255: 7973–7977

    PubMed  CAS  Google Scholar 

  • 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

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Microbiology, Wellcome Research Laboratories, 3030 Cornwallis Road, Research Triangle Park, NC, 27709, USA

    P. Ray & I. Dev

  2. Department of Microbiology, Georgetown University Medical School, Washington, DC, 20007, USA

    C. MacGregor

  3. Department of Microbiology and Immunology, University of North Carolina, School of Medicine, Chapel Hill, NC, 27514, USA

    P. Bassford Jr.

Authors
  1. P. Ray
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. I. Dev
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. C. MacGregor
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. P. Bassford Jr.
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD, 20814-4799, USA

    Henry C. Wu M.D. Ph.D (Professor of Microbiology) (Professor of Microbiology)

  2. Department of Metabolic Regulation, Boston Biomedical Research Institute, 20 Staniford Street, Boston, MA, 02114, USA

    Phang C. Tai Ph.D (Senior Staff Scientist, Associate Professor) (Senior Staff Scientist, Associate Professor)

  3. Department of Microbiology and Molecular Genetics, Harvard Medical School, 23 Shattuck Street, Boston, MA, 02115, USA

    Phang C. Tai Ph.D (Senior Staff Scientist, Associate Professor) (Senior Staff Scientist, Associate Professor)

Rights and permissions

Reprints and permissions

Copyright information

© 1986 Springer-Verlag Berlin · Heidelberg

About this paper

Cite this paper

Ray, P., Dev, I., MacGregor, C., Bassford, P. (1986). Signal Peptidases. In: Wu, H.C., Tai, P.C. (eds) Protein Secretion and Export in Bacteria. Current Topics in Microbiology and Immunology, vol 125. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71251-7_7

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-71251-7_7

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-71253-1

  • Online ISBN: 978-3-642-71251-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation