메뉴 건너뛰기




Volumn 38, Issue 2, 2004, Pages 239-246

Interdependent effects of the charge of the N-terminal region of the signal peptide, SecA, and SecB on secretion of alkaline phosphatase in Escherichia coli

Author keywords

Alkaline phosphatase; Escherichia coli; Protein translocation; SecA; SecB; Signal peptide

Indexed keywords

ALANINE; ALKALINE PHOSPHATASE; CHAPERONE; GLUTAMIC ACID; LYSINE; PROTEIN SUBUNIT; SIGNAL PEPTIDE;

EID: 3543010199     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MBIL.0000023740.66749.b0     Document Type: Article
Times cited : (2)

References (50)
  • 1
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. 1980. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA. 77, 1496-1500.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 2
    • 0035201578 scopus 로고    scopus 로고
    • Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane
    • Muller M., Koch H.G., Beck K., Schafer U. 2001. Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog. Nucleic Acid Res. Mol. Biol. 66, 107-157.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 107-157
    • Muller, M.1    Koch, H.G.2    Beck, K.3    Schafer, U.4
  • 3
    • 0034995184 scopus 로고    scopus 로고
    • The structural basis of protein targeting and translocation in bacteria
    • Driessen A., Manting E., van der Does C. 2001. The structural basis of protein targeting and translocation in bacteria. Nature Struct. Biol. 8, 492-498.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 492-498
    • Driessen, A.1    Manting, E.2    Van Der Does, C.3
  • 4
    • 0025297583 scopus 로고
    • The signal pepide
    • von Heijne G. 1990. The signal pepide. J. Membrane Biol. 115, 195-201.
    • (1990) J. Membrane Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 5
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von Heijne G. 1989. The structure of signal peptides from bacterial lipoproteins. Protein Eng. 2, 531-534.
    • (1989) Protein Eng. , vol.2 , pp. 531-534
    • Von Heijne, G.1
  • 6
    • 0025844917 scopus 로고
    • A de novo designed signal peptide cleavage cassette functions in vivo
    • Nilsson I., von Heijne G. 1991. A de novo designed signal peptide cleavage cassette functions in vivo. J. Biol. Chem. 266, 3408-3410.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3408-3410
    • Nilsson, I.1    Von Heijne, G.2
  • 7
    • 0032502929 scopus 로고    scopus 로고
    • Processing of Escherichia coli alkaline phosphatase: Role of the primary structure of the signal peptide cleavage region
    • Karamyshev A.L., Karamysheva Z.N., Kajava A.V., Ksenzenko V.N., Nesmeyanova M.A. 1998. Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region. J. Mol. Biol. 277, 859-870.
    • (1998) J. Mol. Biol. , vol.277 , pp. 859-870
    • Karamyshev, A.L.1    Karamysheva, Z.N.2    Kajava, A.V.3    Ksenzenko, V.N.4    Nesmeyanova, M.A.5
  • 8
    • 0037184936 scopus 로고    scopus 로고
    • Processing of Escherichia coli alkaline phosphatase: Sequence requirements and possible conformations of the -6 to -4 region of the signal peptide
    • Kajava A.V., Zolov S.N., Pyatkov K.I., Kalinin A.E., Nesmeyanova M.A. 2002. Processing of Escherichia coli alkaline phosphatase: sequence requirements and possible conformations of the -6 to -4 region of the signal peptide. J. Biol. Chem. 277, 50396-50402.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50396-50402
    • Kajava, A.V.1    Zolov, S.N.2    Pyatkov, K.I.3    Kalinin, A.E.4    Nesmeyanova, M.A.5
  • 9
    • 0019982904 scopus 로고
    • On the possible participation of acid phospholipids in the translocation of secreted proteins through the bacterial cytoplasmic membrane
    • Nesmeyanova M.A. 1982. On the possible participation of acid phospholipids in the translocation of secreted proteins through the bacterial cytoplasmic membrane. FEBS Lett. 142, 189-193.
    • (1982) FEBS Lett. , vol.142 , pp. 189-193
    • Nesmeyanova, M.A.1
  • 10
    • 0031043413 scopus 로고    scopus 로고
    • Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphstase provides the secretion efficiency and is involved in the interaction with anionic phospholipids
    • Nesmeyanova M.A., Karamyshev A.L., Karamysheva Z.N., Kalinin A.E., Ksenzenko V.N., Kajava A.V. 1997. Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphstase provides the secretion efficiency and is involved in the interaction with anionic phospholipids. FEBS Lett. 403, 203-207.
    • (1997) FEBS Lett. , vol.403 , pp. 203-207
    • Nesmeyanova, M.A.1    Karamyshev, A.L.2    Karamysheva, Z.N.3    Kalinin, A.E.4    Ksenzenko, V.N.5    Kajava, A.V.6
  • 11
    • 0034193232 scopus 로고    scopus 로고
    • Role of lipids in the translocation of proteins across membranes
    • van Voorst F., de Kruijff B. 2000. Role of lipids in the translocation of proteins across membranes. Biochem. J. 347, 601-612.
    • (2000) Biochem. J. , vol.347 , pp. 601-612
    • Van Voorst, F.1    De Kruijff, B.2
  • 12
    • 0028831186 scopus 로고
    • High selective with low specifity: How SecB has solved the paradox of chaperone binding
    • Randall L.L., Hardy S.D. 1995. High selective with low specifity: how SecB has solved the paradox of chaperone binding. Trends Biochem. Sci. 20, 65-69.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 65-69
    • Randall, L.L.1    Hardy, S.D.2
  • 13
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley A. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57, 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.1
  • 14
    • 0033008601 scopus 로고    scopus 로고
    • Protein targeting to the bacterial cytoplasmic membrane
    • Fekkes P., Driessen A.J. 1999. Protein targeting to the bacterial cytoplasmic membrane. Microbiol. Mol. Biol. Rev. 63, 161-173.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 161-173
    • Fekkes, P.1    Driessen, A.J.2
  • 15
    • 0021867206 scopus 로고
    • Evidence for specificity at an early step in protein export in Escherichia coli
    • Kumamoto C., Beckwith J. 1985. Evidence for specificity at an early step in protein export in Escherichia coli. J. Bacteriol. 163, 267-274.
    • (1985) J. Bacteriol. , vol.163 , pp. 267-274
    • Kumamoto, C.1    Beckwith, J.2
  • 16
    • 0024461843 scopus 로고
    • Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli
    • Kusukawa N., Yura T., Ueguchi C., Akiyama Y., Ito K. 1989. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 8, 3517-3521.
    • (1989) EMBO J. , vol.8 , pp. 3517-3521
    • Kusukawa, N.1    Yura, T.2    Ueguchi, C.3    Akiyama, Y.4    Ito, K.5
  • 17
    • 0025976271 scopus 로고
    • Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli
    • Altman E., Kumamoto C.A., Emr S.D. 1991. Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli. EMBO J. 10, 239-245.
    • (1991) EMBO J. , vol.10 , pp. 239-245
    • Altman, E.1    Kumamoto, C.A.2    Emr, S.D.3
  • 18
    • 0026644011 scopus 로고
    • DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
    • Wild J., Altman E., Yura T., Gross C. 1992. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev. 6, 1165-1172.
    • (1992) Genes Dev. , vol.6 , pp. 1165-1172
    • Wild, J.1    Altman, E.2    Yura, T.3    Gross, C.4
  • 19
    • 0029893301 scopus 로고    scopus 로고
    • Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
    • Wild J., Rossmeissl P., Walter W., Gross, C. 1996. Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli. J. Bacteriol. 178, 3608-3613.
    • (1996) J. Bacteriol. , vol.178 , pp. 3608-3613
    • Wild, J.1    Rossmeissl, P.2    Walter, W.3    Gross, C.4
  • 20
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick J., Hartl F. 1993. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.1    Hartl, F.2
  • 21
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxyterminus of SecA during initiation of precursor protein translocation
    • Fekkes P., van der Does C., Driessen A.J. 1997. The molecular chaperone SecB is released from the carboxyterminus of SecA during initiation of precursor protein translocation. EMBO J. 16, 6105-6113.
    • (1997) EMBO J. , vol.16 , pp. 6105-6113
    • Fekkes, P.1    Van Der Does, C.2    Driessen, A.J.3
  • 23
    • 0020171893 scopus 로고
    • Regulation of a membrane component required for protein secretion in Escherichia coli
    • Oliver D.B., Beckwith J. 1982. Regulation of a membrane component required for protein secretion in Escherichia coli. Cell. 30, 309-311.
    • (1982) Cell , vol.30 , pp. 309-311
    • Oliver, D.B.1    Beckwith, J.2
  • 24
    • 0031962436 scopus 로고    scopus 로고
    • Correlation between requirement for SecA during export and folding properties of precursor polypeptides
    • De Cook H., Randall L. 1998. Correlation between requirement for SecA during export and folding properties of precursor polypeptides. Mol. Microbiol. 27, 469-476.
    • (1998) Mol. Microbiol. , vol.27 , pp. 469-476
    • De Cook, H.1    Randall, L.2
  • 25
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles into the membrane insertion and definition
    • Economou A., Wickner W. 1994. SecA promotes preprotein translocation by undergoing ATP-driven cycles into the membrane insertion and definition. Cell. 78, 835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 26
    • 0032488590 scopus 로고    scopus 로고
    • Interaction between SecA and SecYEG in micellar solution and formation of the membrane-inserted state
    • van der Does C., Manting E.H., Kaufmann A., Lutz M., Driessen A.J. 1998. Interaction between SecA and SecYEG in micellar solution and formation of the membrane-inserted state. Biochemistry. 37, 201-210.
    • (1998) Biochemistry , vol.37 , pp. 201-210
    • Van Der Does, C.1    Manting, E.H.2    Kaufmann, A.3    Lutz, M.4    Driessen, A.J.5
  • 27
    • 0035773932 scopus 로고    scopus 로고
    • The effect of export-specific cytoplasmic chaperone SecB on alkaline phosphatase secretion in Escherichia coli
    • Kononova S., Khokhlova O.V., Zolov S.N., Nesmeyanova M.A. 2001. The effect of export-specific cytoplasmic chaperone SecB on alkaline phosphatase secretion in Escherichia coli. Biokhimiya. 66, 985-990.
    • (2001) Biokhimiya , vol.66 , pp. 985-990
    • Kononova, S.1    Khokhlova, O.V.2    Zolov, S.N.3    Nesmeyanova, M.A.4
  • 28
    • 0042023526 scopus 로고    scopus 로고
    • Interaction of SecB and SecA with the N-terminal region of mature alkaline phosphatase on its secretion in Escherichia coli
    • Khokhlova O.V., Nesmeyanova M.A. 2003. Interaction of SecB and SecA with the N-terminal region of mature alkaline phosphatase on its secretion in Escherichia coli. Mol. Biol. 37, 712-718.
    • (2003) Mol. Biol. , vol.37 , pp. 712-718
    • Khokhlova, O.V.1    Nesmeyanova, M.A.2
  • 29
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu
    • Casadaban M.J. 1976. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu. J. Mol. Biol. 104, 541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 30
    • 0036413921 scopus 로고    scopus 로고
    • Interaction of prePhoA with phospholipids in vivo and in vitro as dependent on the charge of the N-terminal region of the signal peptide and on the membrane content of anionic phospholipids
    • Zolov S.N., Mikhaleva N.I., Kalinin A.E., Nesmeyanova M.A. 2002. Interaction of prePhoA with phospholipids in vivo and in vitro as dependent on the charge of the N-terminal region of the signal peptide and on the membrane content of anionic phospholipids. Biokhimiya. 67, 1051-1060.
    • (2002) Biokhimiya , vol.67 , pp. 1051-1060
    • Zolov, S.N.1    Mikhaleva, N.I.2    Kalinin, A.E.3    Nesmeyanova, M.A.4
  • 31
    • 0002940388 scopus 로고
    • Eds. Gantoni G.L., Davis R. N.Y.: Harper and Row
    • Torriani A. 1966. In: Procedures in Nucleic Acid Research. Eds. Gantoni G.L., Davis R. N.Y.: Harper and Row, 224-234.
    • (1966) Procedures in Nucleic Acid Research , pp. 224-234
    • Torriani, A.1
  • 32
    • 0012904762 scopus 로고    scopus 로고
    • Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes
    • Seoh H., Tai P. 1997. Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes. J. Bacteriol. 179, 1077-1081.
    • (1997) J. Bacteriol. , vol.179 , pp. 1077-1081
    • Seoh, H.1    Tai, P.2
  • 34
    • 0020581487 scopus 로고
    • Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli
    • Michaelis S., Inouye H., Oliver D., Beckwith J. 1983. Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J. Bacteriol. 154, 366-374.
    • (1983) J. Bacteriol. , vol.154 , pp. 366-374
    • Michaelis, S.1    Inouye, H.2    Oliver, D.3    Beckwith, J.4
  • 35
    • 78651153791 scopus 로고
    • Disk electrophoresis. II. Method and application to human serum proteins
    • Davis B. 1964. Disk electrophoresis. II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121, 404-427.
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.1
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of head of bacteriophage T4
    • Laemmli U. 1970. Cleavage of structural protein during the assembly of head of bacteriophage T4. Nature. 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 37
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry O., Rosebrough N., Farr A., Randall R. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.1    Rosebrough, N.2    Farr, A.3    Randall, R.4
  • 38
    • 0019464011 scopus 로고
    • Multiple forms of alkaline phosphatase from Escherichia coli cells with repressed and derepressed biosynthesis of the enzyme
    • Nesmeyanova M., Motlokh O., Kolot M., Kulaev I. 1981. Multiple forms of alkaline phosphatase from Escherichia coli cells with repressed and derepressed biosynthesis of the enzyme. J. Bacteriol. 146, 453-459.
    • (1981) J. Bacteriol. , vol.146 , pp. 453-459
    • Nesmeyanova, M.1    Motlokh, O.2    Kolot, M.3    Kulaev, I.4
  • 39
    • 0029043218 scopus 로고
    • Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in SecA
    • Huie J.L., Silhavy T.J. 1995. Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in SecA. J. Bacteriol. 177, 3518-3526.
    • (1995) J. Bacteriol. , vol.177 , pp. 3518-3526
    • Huie, J.L.1    Silhavy, T.J.2
  • 40
    • 0346686391 scopus 로고    scopus 로고
    • The effects of the membrane phospholipid composition and the charge of the signal peptide on alkaline phosphatase secretion in E. coli
    • Golovastov V.V., Nesmeyanova M.A. 2003. The effects of the membrane phospholipid composition and the charge of the signal peptide on alkaline phosphatase secretion in E. coli. Biokhimiya. 68, 1355-1364.
    • (2003) Biokhimiya , vol.68 , pp. 1355-1364
    • Golovastov, V.V.1    Nesmeyanova, M.A.2
  • 41
    • 0024411967 scopus 로고
    • SecB functions as a cytosolic signal recognition factor for protein export in E. coli
    • Watanabe M., Blobel G. 1989. SecB functions as a cytosolic signal recognition factor for protein export in E. coli. Cell. 58, 695-705.
    • (1989) Cell , vol.58 , pp. 695-705
    • Watanabe, M.1    Blobel, G.2
  • 42
    • 0028883731 scopus 로고
    • High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein
    • Watanabe M., Blobel G. 1995. High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein. Proc. Natl. Acad. Sci. USA. 92, 10133-10136.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10133-10136
    • Watanabe, M.1    Blobel, G.2
  • 44
    • 2642634461 scopus 로고
    • Purified SecB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro
    • Weiss J.B., Ray P.H., Bassford P.J. 1988. Purified SecB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro. Proc. Natl. Acad. Sci. USA. 85, 8978-8982.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8978-8982
    • Weiss, J.B.1    Ray, P.H.2    Bassford, P.J.3
  • 45
    • 0031734169 scopus 로고    scopus 로고
    • The interaction between the chaperone SecB and its ligands: Evidence for multiple subsites for binding
    • Randall L.L., Hardy S.J., Topping T.B., Smith V.F., Bruce J.E., Smith R.D. 1998. The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding. Protein Sci. 7, 2384-2390.
    • (1998) Protein Sci. , vol.7 , pp. 2384-2390
    • Randall, L.L.1    Hardy, S.J.2    Topping, T.B.3    Smith, V.F.4    Bruce, J.E.5    Smith, R.D.6
  • 47
    • 0029796043 scopus 로고    scopus 로고
    • Escherichia coli SecB stimulates export without maintaining export competence of ribose-binding protein signal sequence mutants
    • Francetic O., Kumamoto C.A. 1996. Escherichia coli SecB stimulates export without maintaining export competence of ribose-binding protein signal sequence mutants. J. Bacteriol. 178, 5954-5959.
    • (1996) J. Bacteriol. , vol.178 , pp. 5954-5959
    • Francetic, O.1    Kumamoto, C.A.2
  • 48
    • 0028102530 scopus 로고
    • PrlA and PrlG suppressors reduce the requirement for signal sequence recognition
    • Flower A.M., Doebele R.C., Silhavy T.J. 1994. PrlA and PrlG suppressors reduce the requirement for signal sequence recognition. J. Bacteriol. 176, 5607-5614.
    • (1994) J. Bacteriol. , vol.176 , pp. 5607-5614
    • Flower, A.M.1    Doebele, R.C.2    Silhavy, T.J.3
  • 49
    • 0024525814 scopus 로고
    • Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide
    • Fikes J., Bassford P. 1989. Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide. J. Bacteriol. 171, 402-409.
    • (1989) J. Bacteriol. , vol.171 , pp. 402-409
    • Fikes, J.1    Bassford, P.2
  • 50
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl F.U., Lecker S., Schiebel E., Hendrick J.P., Wickner W. 1990. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell. 63, 269-279.
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.