메뉴 건너뛰기




Volumn 121, Issue 2, 1997, Pages 270-277

The hydrophobic region of signal peptides is a determinant for SRP recognition and protein translocation across the ER membrane

Author keywords

ER translocation; Hydrophobic region; Presecretory protein; Signal peptide; SRP

Indexed keywords

ALANINE; CHIMERIC PROTEIN; LEUCINE; SECRETORY PROTEIN; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE;

EID: 0031045695     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021583     Document Type: Article
Times cited : (54)

References (32)
  • 1
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierasch, L.M. (1989) Signal sequences. Biochemistry 28, 923-930
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 2
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne, G. (1990) The signal peptide. J. Membr. Biol. 115, 195-201
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 3
    • 77957229461 scopus 로고
    • Structural characteristics of presecretory proteins: Their implication as to translocation competency
    • Neupert, W. and Lill, R., eds. Elsevier, Amsterdam
    • Mizushima, S., Tani, K., Hikita, C., and Kato, M. (1992) Structural characteristics of presecretory proteins: their implication as to translocation competency in Membrane Biogenesis and Protein Targeting (Neupert, W. and Lill, R., eds.) pp. 63-74, Elsevier, Amsterdam
    • (1992) Membrane Biogenesis and Protein Targeting , pp. 63-74
    • Mizushima, S.1    Tani, K.2    Hikita, C.3    Kato, M.4
  • 4
    • 0025262033 scopus 로고
    • In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli
    • Sasaki, S., Matsuyama, S., and Mizushima, S. (1990) In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli. J. Biol. Chem. 265, 4358-4363
    • (1990) J. Biol. Chem. , vol.265 , pp. 4358-4363
    • Sasaki, S.1    Matsuyama, S.2    Mizushima, S.3
  • 5
    • 0026701330 scopus 로고
    • Effects of total hydrophobicity and length of the hydrophobic domain of a signal peptide on in vitro translocation efficiency
    • Hikita, C. and Mizushima, S. (1992) Effects of total hydrophobicity and length of the hydrophobic domain of a signal peptide on in vitro translocation efficiency. J. Biol. Chem. 267, 4882-4888
    • (1992) J. Biol. Chem. , vol.267 , pp. 4882-4888
    • Hikita, C.1    Mizushima, S.2
  • 6
    • 0026780329 scopus 로고
    • The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptides
    • Hikita, C. and Mizushima, S. (1992) The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptides. J. Biol. Chem. 267, 12375-12379
    • (1992) J. Biol. Chem. , vol.267 , pp. 12375-12379
    • Hikita, C.1    Mizushima, S.2
  • 7
    • 0025320021 scopus 로고
    • SecA interacts with secretory proteins by recognizing the positive charge at the amino-terminus of the signal peptide in Escherichia coli
    • Akita, M., Sasaki, S., Matsuyama, S., and Mizushima, S. (1990) SecA interacts with secretory proteins by recognizing the positive charge at the amino-terminus of the signal peptide in Escherichia coli. J. Biol. Chem. 265, 8164-8169
    • (1990) J. Biol. Chem. , vol.265 , pp. 8164-8169
    • Akita, M.1    Sasaki, S.2    Matsuyama, S.3    Mizushima, S.4
  • 8
    • 0021417222 scopus 로고
    • The requirement for energy during export, of β-lactamase in Escherichia coli is fulfilled by the total proton motive force
    • Bakker, E.P. and Randall, L.L. (1984) The requirement for energy during export, of β-lactamase in Escherichia coli is fulfilled by the total proton motive force. EMBO J. 3, 895-900
    • (1984) EMBO J. , vol.3 , pp. 895-900
    • Bakker, E.P.1    Randall, L.L.2
  • 9
    • 0022532398 scopus 로고
    • Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles
    • Geller, B.-L., Movva, N.R., and Wickner, W. (1986) Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles. Proc. Natl. Acad. Sci. USA 83, 4219-4222
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4219-4222
    • Geller, B.-L.1    Movva, N.R.2    Wickner, W.3
  • 10
    • 0023654076 scopus 로고
    • In vitro translocation of protein across Escherichia coli membrane vesicles requires both the protein motive force and ATP
    • Yamane, K., Ichihara, S., and Mizushima, S. (1987) In vitro translocation of protein across Escherichia coli membrane vesicles requires both the protein motive force and ATP. J. Biol. Chem. 262, 2358-2362
    • (1987) J. Biol. Chem. , vol.262 , pp. 2358-2362
    • Yamane, K.1    Ichihara, S.2    Mizushima, S.3
  • 11
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P. and Johnson, A.E. (1994) Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 12
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel, B. and Rapoport, T.A. (1995) A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270
    • (1995) Cell , vol.82 , pp. 261-270
    • Jungnickel, B.1    Rapoport, T.A.2
  • 13
    • 0023548385 scopus 로고
    • Engineering of the hydrophobic segment of the signal sequence for efficient secretion of human lysozyme by Saccharomyces cerevisiae
    • Yamamoto, Y., Taniyama, Y., Kikuchi, M., and Ikehara, M. (1987) Engineering of the hydrophobic segment of the signal sequence for efficient secretion of human lysozyme by Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 149, 431-436
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 431-436
    • Yamamoto, Y.1    Taniyama, Y.2    Kikuchi, M.3    Ikehara, M.4
  • 14
    • 0025360748 scopus 로고
    • The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity
    • Bird, P., Gething, M.-J., and Sambrook, J. (1990) The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity. J. Biol. Chem. 265, 8420-8425
    • (1990) J. Biol. Chem. , vol.265 , pp. 8420-8425
    • Bird, P.1    Gething, M.-J.2    Sambrook, J.3
  • 15
    • 0026731437 scopus 로고
    • Conformation and length of the signal sequence affect processing of secretory protein
    • Kohara, A., Yamamoto, Y., and Kikuchi, M. (1992) Conformation and length of the signal sequence affect processing of secretory protein. FEBS Lett. 311, 226-230
    • (1992) FEBS Lett. , vol.311 , pp. 226-230
    • Kohara, A.1    Yamamoto, Y.2    Kikuchi, M.3
  • 16
    • 0028135418 scopus 로고
    • Can a signal sequence become too hydrophobic?
    • Tomilo, M., Wilkinson, K.S., and Ryan, P. (1994) Can a signal sequence become too hydrophobic? J. Biol. Chem. 269, 32016-32021
    • (1994) J. Biol. Chem. , vol.269 , pp. 32016-32021
    • Tomilo, M.1    Wilkinson, K.S.2    Ryan, P.3
  • 17
    • 0018939725 scopus 로고
    • Sequence analysis of mutations that prevent export of λ receptor, an Escherichia coli outer membrane protein
    • Emr, S.D., Hedgpeth, J., Clement, J.-M., Silhavy, T.J., and Hofnung, M. (1980) Sequence analysis of mutations that prevent export of λ receptor, an Escherichia coli outer membrane protein. Nature 285, 82-85
    • (1980) Nature , vol.285 , pp. 82-85
    • Emr, S.D.1    Hedgpeth, J.2    Clement, J.-M.3    Silhavy, T.J.4    Hofnung, M.5
  • 18
    • 0020803631 scopus 로고
    • Importance of secondary structure in the signal sequence for protein secretion
    • Emr, S.D. and Silhavy, T.J. (1983) Importance of secondary structure in the signal sequence for protein secretion. Proc. Natl. Acad. Sci. USA 80, 4599-4603
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4599-4603
    • Emr, S.D.1    Silhavy, T.J.2
  • 19
    • 0021154947 scopus 로고
    • Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide
    • Bankaitis, V.A., Rasmussen, B.A., and Bassford, P.J., Jr. (1984) Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide. Cell 37, 243-252
    • (1984) Cell , vol.37 , pp. 243-252
    • Bankaitis, V.A.1    Rasmussen, B.A.2    Bassford Jr., P.J.3
  • 20
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Fleischer, S. and Fleischer, B., eds. Academic Press, New York
    • Walter, P. and Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation in Methods in Enzymology (Fleischer, S. and Fleischer, B., eds.) Vol. 96, pp. 84-93, Academic Press, New York
    • (1983) Methods in Enzymology , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 21
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Fleischer, S. and Fleischer, B., eds. Academic Press, New York
    • Erickson, A.H. and Blobel, G. (1983) Cell-free translation of messenger RNA in a wheat germ system in Methods in Enzymology (Fleischer, S. and Fleischer, B., eds.) Vol. 96, pp. 38-50, Academic Press, New York
    • (1983) Methods in Enzymology , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 22
    • 0024268344 scopus 로고
    • Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli
    • Yamane, K. and Mizushima, S. (1988) Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 263, 19690-19696
    • (1988) J. Biol. Chem. , vol.263 , pp. 19690-19696
    • Yamane, K.1    Mizushima, S.2
  • 23
    • 0005614190 scopus 로고
    • Photocross-linking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
    • Krieg, U.C., Walter, P., and Johnson, A.E. (1986) Photocross-linking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc. Natl. Acad. Sci. USA 83, 8604-8608
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8604-8608
    • Krieg, U.C.1    Walter, P.2    Johnson, A.E.3
  • 25
    • 0021770917 scopus 로고
    • Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter
    • Melton, D.A., Krieg, P.A., Rebagliati, M.R., Maniatis, T., Zinn, K., and Green, M.R. (1984) Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 12, 7035-7056
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7035-7056
    • Melton, D.A.1    Krieg, P.A.2    Rebagliati, M.R.3    Maniatis, T.4    Zinn, K.5    Green, M.R.6
  • 26
    • 0021010426 scopus 로고
    • Signal recognition particle: A ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties
    • Fleischer, S. and Fleischer, B., eds. Academic Press, New York
    • Walter, P. and Blobel, G. (1983) Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation and properties in Methods in Enzymology (Fleischer, S. and Fleischer, B., eds.) Vol. 96, pp. 682-691, Academic Press, New York
    • (1983) Methods in Enzymology , vol.96 , pp. 682-691
    • Walter, P.1    Blobel, G.2
  • 27
    • 0009499348 scopus 로고
    • Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
    • Walter, P. and Blobel, G. (1980) Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 77, 7112-7116
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7112-7116
    • Walter, P.1    Blobel, G.2
  • 28
    • 0028582033 scopus 로고
    • Inverse relationship of cotranslational translocation with the hydrophobic moment of the bovine preproparathyroid hormone signal sequence
    • Ahn, K., Chen, D., and Kemper, B. (1994) Inverse relationship of cotranslational translocation with the hydrophobic moment of the bovine preproparathyroid hormone signal sequence. Biochim. Biophys. Acta 1224, 459-462
    • (1994) Biochim. Biophys. Acta , vol.1224 , pp. 459-462
    • Ahn, K.1    Chen, D.2    Kemper, B.3
  • 29
    • 0030064680 scopus 로고    scopus 로고
    • A two-step recognition of signal sequences determines the translocation efficiency of proteins
    • Belin, D., Bost, S., Vassalli, V., and Strub, K. (1996) A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J. 15, 468-478
    • (1996) EMBO J. , vol.15 , pp. 468-478
    • Belin, D.1    Bost, S.2    Vassalli, V.3    Strub, K.4
  • 30
    • 0023928974 scopus 로고
    • Transcending the impenetrable: How proteins come to terms with membranes
    • von Heijne, G. (1988) Transcending the impenetrable: how proteins come to terms with membranes. Biochim. Biophys. Acta 947, 307-333
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 307-333
    • Von Heijne, G.1
  • 31
    • 0028101487 scopus 로고
    • The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • Nilsson, I., Whitley, P., and von Heijne, G. (1994) The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell. Biol. 126, 1127-1132
    • (1994) J. Cell. Biol. , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    Von Heijne, G.3
  • 32
    • 0026501551 scopus 로고
    • Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge
    • Sakaguchi, M., Tomiyoshi, R., Kuroiwa, T., Mihara, K., and Omura, T. (1992) Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge. Proc. Natl. Acad. Sci. USA 89, 16-19
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 16-19
    • Sakaguchi, M.1    Tomiyoshi, R.2    Kuroiwa, T.3    Mihara, K.4    Omura, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.