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  • 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: 32413245.
  • Allsop AE, Brooks G, Bruton G, Coulton S, Edwards PD, Hatton IK, Kaura AC, McLean SD, Pearson ND, Smale TC, Southgate R. 1995. Penem inhibitors of bacterial signal peptidase. Bioorg Med Chem Lett 5: 443448.
  • Baker RK, Lively MO. 1987. Purification and characterization of chicken oviduct microsomal signal peptidase. Biochemistry 26: 85618567.
  • 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: 12311238.
  • Bassford P, Beckwith J. 1979. Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm. Nature 277 538541.
  • 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: 7881.
  • 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: 167176.
  • 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: 27172722.
  • Black MT, Munn JG, Allsop AE. 1992. On the catalytic mechanism of prokaryotic leader peptidase 1. Biochem J 282: 539543.
  • 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: 49574961.
  • Böhni PC, Deshaies RJ, Schekman RW. 1988. SECI 1 is required for signal peptide processing and yeast cell growth. J Cell Biol 106: 10351042.
  • 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: 605618.
  • Bult CJ, White O, Olsen GJ, Zhou L, Fleischmann RD, Sutton GG, Blake JA, FitzGerald LM, Clayton RA, Gocayne JD, Kerlavage AR, Dougherty BA, Tomb JF, Adams MD, Reich CI, Overbeek R, Kirkness EF, Weinstock KG, Merrick JM, Glodek A, Scott JL, Geoghagen NSM, Weidman JF, Fuhrmann JL, Nguyen D, Utterback TR, Kelley JM, Peterson JD, Sadow PW, Hanna MC, Cotton MD, Roberts KM, Hurst MA, Kaine BP, Borodovsky M, Klenk HP, Fraser CM, Smith HO, Woese CR, Venter JC. 1996. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273: 10581073.
  • Carlson M, Botstein D. 1982. Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28: 145154.
  • Chabin R, Green BG, Gale P, Maycock AL, Weston H, Dorn CP, Finke PE, Hagmann WK, Hale JJ, MacCoss M, Shah SK, Underwood D, Doherty JB, Knight WB. 1993. Mechanism of inhibition of human leucocyte elastase by monocyclic beta-lactams. Biochemistry 32: 89708980.
  • Chatterjee S, Suciu D, Dalbey RE, Kahn PC, Inouye M. 1995. Determination of Km and kcat for signal peptidase I using a full length secretory precursor, pro-OmpA-nuclease A. J Mol Biol 245: 311314.
  • 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: 57125718.
  • Dalbey RE, von Heijne G. 1992. Signal peptidases in prokaryotes and eukaryotes—A new protease family. (Trends Biochem Sci 17: 474478.
  • 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: 1592515931.
  • Date T. 1983. Demonstration by a novel genetic technique that leader peptidase is an essential enzyme of Escherichia coli. J Bacteriol 154: 7683.
  • 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: 61066110.
  • Dev IK, Ray PH, Novak P. 1990. Minimum substrate sequence for signal peptidase I of Escherichia coli. J Biol Chem 265: 2006920072.
  • Dierstein R, Wickner W. 1986. Requirements for substrate recognition by bacterial leader peptidase. EMBO J 5: 427431.
  • Emr SD, Schwartz 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: 58025806.
  • Emr SD, Silhavy TJ. 1980. Mutations affecting localization of an Escherichia coli outer membrane protein, the bacteriophage lambda receptor. J Mol Biol 141: 6390.
  • Evans EA, Gilmore R, Blobel G. 1986. Purification of microsomal signal peptidase as a complex. Proc Natl Acad Sci USA 83: 581585.
  • 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 271: 1646016465.
  • 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: 34173423.
  • Fikes JD, Bassford PJ Jr. 1987. Export of unprocessed precursor maltosebinding protein to the periplasm of Escherichia coli cells. J Bacteriol 169: 23522359.
  • Fleischmann RD, Adam MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb J-F, Dougherty BA, Merrick JM, McKenney K, Sutton G, FitzHugh W, Fields CA, Gocayne JD, Scott JD, Shirley R, Liu L-I, Glodek A, Kelley JM, Weidman JF, Philips CA, Spriggs T, Hedblom E, Cotton MD, Utterback TR, Hanna MC, Nguyen DT, Saudek DM, Brandon RC, Fine LD, Fritchman JL, Fuhrmann JL, Geoghagen NSM, Ghehm CL, McDonald LA, Small KV, Fraser CM, Smith HO, Venter JC. 1995. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269: 496512.
  • 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: 20702078.
  • Fraser CM, Gocayne JD, White O, Adam MD, Clayton RA, Fleischmann RD, Bult CJ, Kerlavage AR, Sutton G, Kelley JM, Fritchman JL, Weidman JF, Small KV, Sandusky M, Fuhrmann J, Nguyen D, Utterback TR, Saudek DM, Phillips CA, Merrick JM, Tomb J-F, Dougherty BA, Bott KF, Hu P-C, Lucier TS, Peterson SN, Smith HO, Hutchison III CA, Venter JC. 1995. The minimal gene complement of Mycoplasma genitalium. Science 270: 397403
  • Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldman H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG. 1996. Life with 6000 genes. Science 274: 546567.
  • Greenburg G, Blobel G. 1994. cDNA-derived primary structure of the 25-kDa subunit of canine microsomal signal peptidase complex. J Biol Chem 269: 2535425358.
  • Greenburg G, Shelness GS, Blobel G. 1989. A subunit of mammalian signal peptidase is homologous to yeast SECI 1 protein. J Biol Chem 264: 1576215765.
  • 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: 39173921.
  • Haugen TH, Heath EC. 1979. De novo biosynthesis of an enzymatically active precursor form of bovine pancreatic RNase. Proc Natl Acad Sci USA 76: 26892693.
  • 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: 6468.
  • Inada T, Court DL, Ito K, Nakamura Y. 1989. Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli. J Bacteriol 171: 585587.
  • Ito K. 1982. Purification of the precursor form of maltose-binding protein, a periplasmic protein of Escherichia coli. J Biol Chem 257: 98959897.
  • Jackson RC. 1983. Quantitative assay for signal peptidase. Methods Enzymol 96: 784794.
  • Jackson RC, Blobel G. 1977. Post-translational cleavage of presccretory proteins with an extract of rough microsomes from canine pancreas containing signal peptidase activity. Proc Natl Acad Sci USA 74: 55985602.
  • Jackson RC, Blobel G. 1980. Post-translational processing of full-length presecretory proteins with canine pancreatic signal peptidase. Ann NY Acad Sci 343: 391404.
  • 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: 25452550.
  • Kalies KU, Hartmann E. 1996. Membrane topology of the 12– and 25-kDa subunits of the mammalian signal peptidase complex. J Biol Chem 271: 39253929.
  • Kaschnitz R, Kreil G. 1978. Processing of prepromelittin by subcellular fractions from rat liver. Biochem Biophys Res Commun 83: 901907.
  • Kiwin 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: 1638616390.
  • 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: 903914.
  • Kuhn A, Wickner W. 1985. Conserved residues of the leader peptide are essential for cleavage by leader peptidase. J Biol Chem 260: 1591415918.
  • 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: 83478354.
  • 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: 274280.
  • Lin LL, Little JW. 1989. Autodigestion and RecA-dependent cleavage of Indmutant LexA proteins. J Mol Biol 210: 439452.
  • Little JW. 1993. LexA cleavage and other self-processing reactions. J Bacteriol 175: 49434950.
  • Lively MO, Newsome AL, Nusier M. 1994. Eukaryote microsomal signal peptidases. Methods Enzymol 244: 301314.
  • Lively MO, Walsh KA. 1983. Hen oviduct signal peptidase is an integral membrane protein. J Biol Chem 258: 94889495.
  • 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 176: 621631.
  • Michaelis S, Beckwith J. 1982. Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu Rev Microbiol 36: 435465.
  • Milstein C, Brownlee GG, Harrison TM, Mathews MB. 1972. A possible precursor of immunoglobulin light chains. Nat New Biol 239: 117120.
  • Moore KE, Miura S. 1987. A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli. J Biol Chem 262: 88068813.
  • Müller P, Ahrens K, Keller T, Klaucke A. 1995. A TnphoA insertion within the Bradyrhizobium japonicum sips gene, homologous to prokaryotic signal peptidases, results in extensive changes in the expression of PBM-specific nodulins of infected soybean (Glycine max) cells. Mol Microbiol 18: 831840.
  • 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: 1713917147.
  • 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: 2909429099.
  • Newsome AL, McLean JW, Lively MO. 1992. Molecular cloning of a cDNA encoding the glycoprotein of hen oviduct microsomal signal peptidase. Biochem J 282: 447452.
  • 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: 16.
  • 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: 165177.
  • 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: 243246.
  • Nunnari J, Fox TD, Walter P. 1993. A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262: 19972004.
  • 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: 199204.
  • Paetzel M, Chernaia M, Strynadka N, Tschantz W, Cao G, Dalbey RE, James MN. 1995. Crystallization of a soluble, catalytically active form of Escherichia coli leader peptidase. Proteins Struct Func Genet 23: 122125.
  • Peat TS, Frank EG, McDonald JP, Levine AS, Woodgate R, Hendrickson WA. 1996. Structure of the UmuD' protein and its regulation in response to DNA damage. Nature 380: 727730
  • Philipp WJ, Poulet S, Eiglmeier K, Pascopella L, Balasubramanian V, Heym B, Bergh S, Bloom BR, Jacobs WR, Cole ST. 1996. An integrated map of the genome of the tubercle bacillus, Mycobacterium tuberculosis H37Rv, and comparison with Mycobacterium leprae. Proc Natl Acad Sci USA 93: 31323137.
  • 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: 13131317.
  • 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 268: 57355740.
  • Roland KL, Little JW. 1990. Reaction of LexA repressor with diisopropyl flu-orophosphate. A test of the serine protease model. J Biol Chem 265: 1282812835.
  • 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: 247254.
  • Schneider A, Oppliger W, Jeno P. 1994. Purified inner membrane protease I of yeast mitochondria is a heterodimer. J Biol Chem 269: 86358638.
  • 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: 1215212156.
  • Shelness GS, Blobel G. 1990. Two subunits of the canine signal peptidase complex are homologous to yeast SECI 1 protein. J Biol Chem 265: 95129519.
  • Shelness GS, Kanwar YS, Blobel G. 1988. cDNA-derived primary structure of the glycoprotein component of canine microsomal signal peptidase complex. J Biol Chem 263: 1706317070.
  • Shelness GS, Lin L, Nicchitta CV. 1993. Membrane topology and biogenesis of eukaryotic signal peptidase. J Biol Chem 268: 52015208.
  • 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: 1177511781.
  • Signs SA, Jacquet R. 1994. Induction of ethanol dependence increases signal peptidase mRNA levels in rat brain. Mol Cell Biochem 139: 2126.
  • Sung M, Dalbey RE. 1992. Identification of potential active-site residues in the Escherichia coli leader peptidase. J Biol Chem 267: 1315413159.
  • 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 73: 11791183.
  • Talmadge K, Kaufman J, Gilbert W. 1980. Bacteria mature preproinsulin to proinsulin. Proc Natl Acad Sci USA 77: 39883992.
  • 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 34: 39353941.
  • 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 268: 2734927354.
  • 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: 28192828.
  • 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: 36113618.
  • 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: 5561.
  • van Dijl JM, van den Bergh R, Reversma T, Smith H, Bron S, Venema G. 1990. Molecular cloning of the Salmonella typhimurium lep gene in Escherichia coli. Mol Gen Genet 223: 233240.
  • 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: 207214.
  • von Heijne G. 1983. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 116: 1721.
  • von Heijne G. 1985. Signal sequences. The limits of variation. J Mol Biol 184: 99105.
  • von Heijne G. 1994. Signal peptidase. Austin, Texas: R.G. Landes Company.
  • 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: 28092813.
  • 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 32: 85348539.
  • Wickner W, Moore K, Dibb N, Geissert D, Rice M. 1987. Inhibition of purified Escherichia coli leader peptidase by the leader (signal) peptide of bacterio-phage M13 procoat. J Bacteriol 169: 38213822.
  • Wolfe PB, Silver P, Wickner W. 1982. The isolation of homogeneous leaderpeptidase from a strain of Escherichia coli which overproduces the enzyme. J Biol Chem 257: 78987902.
  • 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 258: 1207312080.
  • YaDeau JT, Blobel G. 1989. Solubilization and characterization of yeast signal peptidase. J Biol Chem 264: 29282934.
  • YaDeau JT, Klein C, Blobel G. 1991. Yeast signal peptidase contains a glyco-protein and the Sec 11 gene product. Proc Natl Acad Sci USA 88: 517521.
  • 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: 35933597.
  • Zwizinski C, Wickner W. 1980. Purification and characterization of leader (signal) peptidase from Escherichia coli. J Biol Chem 255: 79737977.