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Volumn 139, Issue 7, 1997, Pages 1697-1708

Regulation of the ribosome-membrane junction at early stages of presecretory protein translocation in the mammalian endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; SECRETORY PROTEIN; SIGNAL PEPTIDE;

EID: 0031417386     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.7.1697     Document Type: Article
Times cited : (12)

References (52)
  • 1
    • 0023730553 scopus 로고
    • Penetration of the signal sequence of the Eschericia coli PhoE protein into phospholipid model membranes leads to lipid specific changes in signal peptide structure and alterations of lipid structure
    • Batenburg, A.M., R.A. Demel, A.J. Verkleij, and B. de Kruif. 1988. Penetration of the signal sequence of the Eschericia coli PhoE protein into phospholipid model membranes leads to lipid specific changes in signal peptide structure and alterations of lipid structure. Biochemistry. 27:5678-5685.
    • (1988) Biochemistry , vol.27 , pp. 5678-5685
    • Batenburg, A.M.1    Demel, R.A.2    Verkleij, A.J.3    De Kruif, B.4
  • 2
    • 0023607313 scopus 로고
    • Translocation in yeast and mammalian cells: Not all signal sequences are functionally equivalent
    • Bird, P., M.J. Gething, and J. Sambrook. 1987. Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent. J. Cell Biol. 105:2905-2914.
    • (1987) J. Cell Biol. , vol.105 , pp. 2905-2914
    • Bird, P.1    Gething, M.J.2    Sambrook, J.3
  • 3
    • 0016752682 scopus 로고
    • Transfer of proteins across membranes II. reconstitution of functional rough microsomes from heterologous components
    • Blobel, G., and B. Dobberstein. 1975. Transfer of proteins across membranes II. reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67:852-862.
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 4
    • 0016203040 scopus 로고
    • A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels
    • Bonner, W.M., and R.A. Laskey. 1974. A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels. Eur. J. Biochem. 46:83-88.
    • (1974) Eur. J. Biochem. , vol.46 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 5
    • 0028822223 scopus 로고
    • BiP and Sec63p are required for both cotranslational and posttranslational translocation into the yeast endoplasmic reticulum
    • Brodsky, J.L., J. Goeckler, and R. Schekman. 1995. BiP and Sec63p are required for both cotranslational and posttranslational translocation into the yeast endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 92:9643-9646.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9643-9646
    • Brodsky, J.L.1    Goeckler, J.2    Schekman, R.3
  • 6
    • 0022415759 scopus 로고
    • In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides
    • Briggs, M.S., L.M. Gierasch, A. Zlotnick, J.D. Lear, and W.F. DeGrado. 1985. In vivo function and membrane binding properties are correlated for Escherichia coli LamB signal peptides. Science. 228:1096-1099.
    • (1985) Science , vol.228 , pp. 1096-1099
    • Briggs, M.S.1    Gierasch, L.M.2    Zlotnick, A.3    Lear, J.D.4    DeGrado, W.F.5
  • 7
    • 0025312051 scopus 로고
    • Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides
    • Chou, M.M., and D.A. Kendall. 1990. Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides. J. Biol. Chem. 265:2873-2880.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2873-2880
    • Chou, M.M.1    Kendall, D.A.2
  • 8
    • 0023026186 scopus 로고
    • Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein
    • Connolly, T., and R. Gilmore. 1986. Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein. J. Cell Biol. 129:2253-2261.
    • (1986) J. Cell Biol. , vol.129 , pp. 2253-2261
    • Connolly, T.1    Gilmore, R.2
  • 9
    • 0024507257 scopus 로고
    • Access of proteinase K to partially translocated nascent polypeptides in intact and detergent-solubilized membranes
    • Connolly, T., P. Collins, and R. Gilmore. 1989. Access of proteinase K to partially translocated nascent polypeptides in intact and detergent-solubilized membranes. J. Cell Biol. 108:299-307.
    • (1989) J. Cell Biol. , vol.108 , pp. 299-307
    • Connolly, T.1    Collins, P.2    Gilmore, R.3
  • 10
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K.S., S. Liao, V.W. Worrell, G.D. Reinhart, and A.E. Johnson. 1994. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell. 78:461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.W.3    Reinhart, G.D.4    Johnson, A.E.5
  • 11
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a non-cyloplasmic aqueous environment at the ER membrane early in translocation
    • Crowley, K.S., G.D. Reinhart, and A.E. Johnson. 1993. The signal sequence moves through a ribosomal tunnel into a non-cyloplasmic aqueous environment at the ER membrane early in translocation. Cell. 73:1101-1115.
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3
  • 12
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierasch, L. 1989. Signal sequences. Biochemistry. 28:923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.1
  • 13
    • 0022129497 scopus 로고
    • Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants
    • Gilmore, R., and G. Blobel. 1985. Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants. Cell. 42:497-505.
    • (1985) Cell , vol.42 , pp. 497-505
    • Gilmore, R.1    Blobel, G.2
  • 14
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in translocation
    • Görlich, D., E. Hartmann, S. Prehn, and T.A. Rapopori. 1992a. A protein of the endoplasmic reticulum involved early in translocation. Nature. 357:47-52.
    • (1992) Nature , vol.357 , pp. 47-52
    • Görlich, D.1    Hartmann, E.2    Prehn, S.3    Rapopori, T.A.4
  • 15
    • 0026466143 scopus 로고
    • A mammalian homolog of Sec61p and SecYp is associated with ribosomes and nascent polypeptides during translocation
    • Görlich, D., S. Prehn, E. Hartmann, K.-U. Kalies, and T.A. Rapoport. 1992b. A mammalian homolog of Sec61p and SecYp is associated with ribosomes and nascent polypeptides during translocation. Cell. 71:489-503.
    • (1992) Cell , vol.71 , pp. 489-503
    • Görlich, D.1    Prehn, S.2    Hartmann, E.3    Kalies, K.-U.4    Rapoport, T.A.5
  • 17
    • 0024451880 scopus 로고
    • A membrane component of the endoplasmic reticulum that may be essential for protein translocation
    • Hartmann, E., M. Wiedmann, and T.A. Rapoport. 1989. A membrane component of the endoplasmic reticulum that may be essential for protein translocation. EMBO (Eur. Mol. Biol. Organ.) J. 8:2225-2229.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 2225-2229
    • Hartmann, E.1    Wiedmann, M.2    Rapoport, T.A.3
  • 18
    • 0029924441 scopus 로고    scopus 로고
    • Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol
    • Hegde, R.S., and V.R. Lingappa. 1996. Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol. Cell. 85:217-228.
    • (1996) Cell , vol.85 , pp. 217-228
    • Hegde, R.S.1    Lingappa, V.R.2
  • 20
    • 0025721096 scopus 로고
    • Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function
    • Hoy, D.W., and L.M. Gierasch. 1991. Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function. Biochemistry. 30:10156-10163.
    • (1991) Biochemistry , vol.30 , pp. 10156-10163
    • Hoy, D.W.1    Gierasch, L.M.2
  • 21
    • 0021004695 scopus 로고
    • Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA
    • Jackson, R.J., and T. Hunt. 1983. Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA. Methods Enzymol. 96:50-73.
    • (1983) Methods Enzymol. , vol.96 , pp. 50-73
    • Jackson, R.J.1    Hunt, T.2
  • 22
    • 0027993450 scopus 로고
    • Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence
    • Jones, J.D., and L. Gierasch. 1994a. Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence. Biophys. J. 67:1546-1561.
    • (1994) Biophys. J. , vol.67 , pp. 1546-1561
    • Jones, J.D.1    Gierasch, L.2
  • 23
    • 0028142681 scopus 로고
    • Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein
    • Jones, J.D., and L.M. Gierasch. 1994b. Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein. Biophys. J. 67:1534-1545.
    • (1994) Biophys. J. , vol.67 , pp. 1534-1545
    • Jones, J.D.1    Gierasch, L.M.2
  • 24
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel, B., and T.A. Rapoport. 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
  • 25
    • 0024425706 scopus 로고
    • Protein translocation across the endoplasmic reticulum membrane: Identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel
    • Krieg, U.C., A.E. Johnson, and P. Walter. 1989. Protein translocation across the endoplasmic reticulum membrane: identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel. J. Cell Biol. 109:2033-2043.
    • (1989) J. Cell Biol. , vol.109 , pp. 2033-2043
    • Krieg, U.C.1    Johnson, A.E.2    Walter, P.3
  • 26
    • 0022527444 scopus 로고
    • The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle
    • Kurzchalia, T.V., M. Wiedmann, A.S. Girshovich, E.S. Bochkareva, H. Bielka, and T.A. Rapoport. 1986. The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle. Nature. 320: 634-636.
    • (1986) Nature , vol.320 , pp. 634-636
    • Kurzchalia, T.V.1    Wiedmann, M.2    Girshovich, A.S.3    Bochkareva, E.S.4    Bielka, H.5    Rapoport, T.A.6
  • 27
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., J. Lin, H. Do, and A.W. Johnson. 1997. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell. 90:31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.W.4
  • 28
    • 0028809495 scopus 로고
    • Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae
    • Lyman, S.K., and R. Schekman. 1995. Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae. J. Cell Biol. 131:1163-1171.
    • (1995) J. Cell Biol. , vol.131 , pp. 1163-1171
    • Lyman, S.K.1    Schekman, R.2
  • 29
    • 0014202553 scopus 로고
    • Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding
    • Malkin, L.I., and A. Rich. 1967. Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding. J. Mol. Biol. 26:329-346.
    • (1967) J. Mol. Biol. , vol.26 , pp. 329-346
    • Malkin, L.I.1    Rich, A.2
  • 30
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., M.W. Hofmann, J. Brunner, and B. Dobberstein. 1995. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell. 81:201-214.
    • (1995) Cell , vol.81 , pp. 201-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 32
    • 0030846015 scopus 로고    scopus 로고
    • Identification of a novel stage of ribosome/nascent chain association with the endoplasmic reticulum membrane
    • Murphy, E.G. III., T. Zheng, and C.V. Nicchitta. 1997. Identification of a novel stage of ribosome/nascent chain association with the endoplasmic reticulum membrane. J. Cell Biol. 136:1213-1226.
    • (1997) J. Cell Biol. , vol.136 , pp. 1213-1226
    • Murphy III, E.G.1    Zheng, T.2    Nicchitta, C.V.3
  • 33
    • 0024604382 scopus 로고
    • Nascent chain binding and translocation are distinct processes: Differentiation by chemical alkylation
    • Nicchitta, C.V., and G. Blobel. 1989. Nascent chain binding and translocation are distinct processes: differentiation by chemical alkylation. J. Cell Biol. 108:789-795.
    • (1989) J. Cell Biol. , vol.108 , pp. 789-795
    • Nicchitta, C.V.1    Blobel, G.2
  • 34
    • 0025019704 scopus 로고
    • Assembly of translocation-competent proteoliposomes form detergent solubilized rough microsomes
    • Nicchitta, C.V., and G. Blobel. 1990. Assembly of translocation-competent proteoliposomes form detergent solubilized rough microsomes. Cell. 60:259-269.
    • (1990) Cell , vol.60 , pp. 259-269
    • Nicchitta, C.V.1    Blobel, G.2
  • 35
    • 0026086579 scopus 로고
    • Reconstitution of secretory protein translocation from detergent-solubilized rough microsomes
    • Nicchitta, C.V., G. Migliaccio, and G. Blobel. 1991. Reconstitution of secretory protein translocation from detergent-solubilized rough microsomes. Methods Cell Biol. 34:263-285.
    • (1991) Methods Cell Biol. , vol.34 , pp. 263-285
    • Nicchitta, C.V.1    Migliaccio, G.2    Blobel, G.3
  • 36
    • 0027238583 scopus 로고
    • Lumenal proteins of the endoplasmic reticulum are required to complete protein translocation
    • Nicchitta, C.V., and G. Blobel. 1993. Lumenal proteins of the endoplasmic reticulum are required to complete protein translocation. Cell. 73:989-998.
    • (1993) Cell , vol.73 , pp. 989-998
    • Nicchitta, C.V.1    Blobel, G.2
  • 37
    • 0029073398 scopus 로고
    • Stage and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane
    • Nicchitta, C.V., E.C. Murphy, R. Haynes, and G.S. Shelness. 1995. Stage and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane. J. Cell Biol. 129:957-970.
    • (1995) J. Cell Biol. , vol.129 , pp. 957-970
    • Nicchitta, C.V.1    Murphy, E.C.2    Haynes, R.3    Shelness, G.S.4
  • 38
    • 0017187839 scopus 로고
    • V. Magnesium-dependent dissociation of tight couples into subunits: Measurements of dissociation constants and exchange rates
    • Noll, M., and H. Noll. 1976. V. Magnesium-dependent dissociation of tight couples into subunits: measurements of dissociation constants and exchange rates. J. Mol. Biol. 105:111-130.
    • (1976) J. Mol. Biol. , vol.105 , pp. 111-130
    • Noll, M.1    Noll, H.2
  • 39
    • 0025012428 scopus 로고
    • The 54K protein of signal recognition particle contains a methionine-rich RNa binding domain
    • Romisch, K., J. Webb, K. Lingelbach, H. Gausepohl, and B. Dobberstein. 1990. The 54K protein of signal recognition particle contains a methionine-rich RNA binding domain. J. Cell Biol. 111:1793-1802.
    • (1990) J. Cell Biol. , vol.111 , pp. 1793-1802
    • Romisch, K.1    Webb, J.2    Lingelbach, K.3    Gausepohl, H.4    Dobberstein, B.5
  • 40
    • 85010245118 scopus 로고
    • On the attachment of ribosomes to microsomal membranes
    • Sahatini, D.D., Y. Tashiro, and G.E. Palade. 1966. On the attachment of ribosomes to microsomal membranes. J. Mol. Biol. 19:503-524.
    • (1966) J. Mol. Biol. , vol.19 , pp. 503-524
    • Sahatini, D.D.1    Tashiro, Y.2    Palade, G.E.3
  • 41
    • 0026589260 scopus 로고
    • Sec61p and BiP directly facilitate polypeptide translocation into the ER
    • Sanders, S.L., K.M. Whitfield, J.P. Vogel, M.D. Rose, and R.W. Schekman, 1992. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell. 69:353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.L.1    Whitfield, K.M.2    Vogel, J.P.3    Rose, M.D.4    Schekman, R.W.5
  • 42
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. Von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 43
    • 0023737896 scopus 로고
    • Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum
    • Shaw, A., P.J.M. Rottier, and J.K. Rose. 1988. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 85:7592-7596.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7592-7596
    • Shaw, A.1    Rottier, P.J.M.2    Rose, J.K.3
  • 44
    • 0029951178 scopus 로고    scopus 로고
    • Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum
    • Voigt, S., B. Jungnickel, E. Hartmann, and T.A. Rapoport. 1996. Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum. J. Cell Biol. 134:25-35.
    • (1996) J. Cell Biol. , vol.134 , pp. 25-35
    • Voigt, S.1    Jungnickel, B.2    Hartmann, E.3    Rapoport, T.A.4
  • 45
    • 0021770334 scopus 로고
    • How signal sequences maintain cleavage specificity
    • von Heinje, G. 1984. How signal sequences maintain cleavage specificity. J. Mol. Biol. 173:243-251.
    • (1984) J. Mol. Biol. , vol.173 , pp. 243-251
    • Von Heinje, G.1
  • 46
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • von Heinje, G. 1985. Signal sequences. The limits of variation. J. Mol. Biol. 184: 99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heinje, G.1
  • 47
    • 0019849075 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in vitro-assembled polysomes synthesizing secretory proteins
    • Walter, P., I. Ibrahimi, and G. Blobel. 1981a. Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in vitro-assembled polysomes synthesizing secretory proteins. J. Cell Biol. 91: 545-550.
    • (1981) J. Cell Biol. , vol.91 , pp. 545-550
    • Walter, P.1    Ibrahimi, I.2    Blobel, G.3
  • 48
    • 0019817924 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in vitro-assembled polysomes synthesizing secretory proteins
    • Walter, P., and G. Blobel. 1981b. Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in vitro-assembled polysomes synthesizing secretory proteins. J. Cell Biol. 91:551-556.
    • (1981) J. Cell Biol. , vol.91 , pp. 551-556
    • Walter, P.1    Blobel, G.2
  • 49
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P., and G. Blobel. 1983. Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96:84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 50
    • 0015999584 scopus 로고
    • Assay of reassociation of eukaryotic ribosomal subunits catalyzed by initiation factors
    • Wettenhall, R.E.H., and I.G. Wool. 1974. Assay of reassociation of eukaryotic ribosomal subunits catalyzed by initiation factors. Methods Enzymol. 30: 186-197.
    • (1974) Methods Enzymol. , vol.30 , pp. 186-197
    • Wettenhall, R.E.H.1    Wool, I.G.2
  • 51
    • 0023192259 scopus 로고
    • A signal sequence receptor in the endoplasmic reticulum membrane
    • Wiedmann, M., T.V. Kurzchalia, E. Hartmann, and T.A. Rapoport. 1987. A signal sequence receptor in the endoplasmic reticulum membrane. Nature. 328: 830-833.
    • (1987) Nature , vol.328 , pp. 830-833
    • Wiedmann, M.1    Kurzchalia, T.V.2    Hartmann, E.3    Rapoport, T.A.4
  • 52
    • 0025601549 scopus 로고
    • The methioninerich domain of the 54kd protein subunit of the signal recognition particle contains an RNa binding site and can be crosslinked to a signal sequence
    • Zopf, D., H.D. Bernstein, A.E. Johnson, and P. Walter. 1990. The methioninerich domain of the 54kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO (Eur. Mol. Biol. Organ.) J. 9:4511-4517.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 4511-4517
    • Zopf, D.1    Bernstein, H.D.2    Johnson, A.E.3    Walter, P.4


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