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Volumn 89, Issue 5, 1997, Pages 703-713

Empty site forms of the SRP54 and SRα GTPase mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MESSENGER RNA; SIGNAL RECOGNITION PARTICLE;

EID: 0030678106     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80253-6     Document Type: Article
Times cited : (108)

References (39)
  • 1
    • 0028125253 scopus 로고
    • The SRP54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe
    • Althoff, S.M., Stevens, S.W., and Wise, J.A. (1994). The SRP54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe. Mol. Cell. Biol. 14, 7839-7854.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7839-7854
    • Althoff, S.M.1    Stevens, S.W.2    Wise, J.A.3
  • 2
    • 0024523481 scopus 로고
    • Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor
    • Andrews, D.W., Lauffer, L., Walter, P., and Lingappa, V.R. (1989). Evidence for a two-step mechanism involved in assembly of functional signal recognition particle receptor. J. Cell Biol. 108, 797-810.
    • (1989) J. Cell Biol. , vol.108 , pp. 797-810
    • Andrews, D.W.1    Lauffer, L.2    Walter, P.3    Lingappa, V.R.4
  • 3
    • 0029963973 scopus 로고    scopus 로고
    • Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
    • Bacher, G., Lütcke, H., Jungnickel, B., Rapoport, T.A., and Dobberstein, B. (1996). Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Nature 381, 248-251.
    • (1996) Nature , vol.381 , pp. 248-251
    • Bacher, G.1    Lütcke, H.2    Jungnickel, B.3    Rapoport, T.A.4    Dobberstein, B.5
  • 4
    • 0024966540 scopus 로고
    • The amino acid sequence of the 54 kDa subunit of the signal recognition particle suggests a model for signal sequence recognition
    • Bernstein, H.D., Poritz, M.A., Strub, K., Hoben, P.J., Brenner, S., and Walter, P. (1989). The amino acid sequence of the 54 kDa subunit of the signal recognition particle suggests a model for signal sequence recognition. Nature 340, 482-486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 5
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H.R., Sanders, D.A., and McCormick, F. (1990). The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 6
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A., and McCormick, F. (1991). The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 7
    • 0023026186 scopus 로고
    • Formation of a functional ribosome-membrane junction during protein translocation requires the participation of a GTP-binding protein
    • Connolly, T., and Gilmore, R. (1986). Formation of a functional ribosome-membrane junction during protein translocation requires the participation of a GTP-binding protein. J. Cell Biol. 103, 2253-2261.
    • (1986) J. Cell Biol. , vol.103 , pp. 2253-2261
    • Connolly, T.1    Gilmore, R.2
  • 8
    • 0024973846 scopus 로고
    • The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide
    • Connolly, T., and Gilmore, R. (1989). The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide. Cell 57, 599-610.
    • (1989) Cell , vol.57 , pp. 599-610
    • Connolly, T.1    Gilmore, R.2
  • 9
    • 0027361668 scopus 로고
    • GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor
    • Connolly, T., and Gilmore, R. (1993). GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor. J. Cell Biol. 123, 799-807.
    • (1993) J. Cell Biol. , vol.123 , pp. 799-807
    • Connolly, T.1    Gilmore, R.2
  • 10
    • 0026326816 scopus 로고
    • Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor
    • Connolly, T., Rapiejko, P.J., and Gilmore, R. (1991). Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor. Science 252, 1171-1173.
    • (1991) Science , vol.252 , pp. 1171-1173
    • Connolly, T.1    Rapiejko, P.J.2    Gilmore, R.3
  • 11
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • Crowley, K.S., Reinhart, G.D., and Johnson, A.E. (1993). The signal sequence moves through a ribosomal tunnel into a noncytoplasmic 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
    • 0031017523 scopus 로고    scopus 로고
    • Structure of the conserved GTPase domain of the signal recognition particle
    • Freymann, D.M., Keenan, R.J., Stroud, R.M., and Walter, P. (1997). Structure of the conserved GTPase domain of the signal recognition particle. Nature 258, 361-364.
    • (1997) Nature , vol.258 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 13
    • 0021014636 scopus 로고
    • Transient involvement of the gnal recognition particle and its receptor in the microsomal membrane prior to protein translocation
    • Gilmore, R., and Blobel, G. (1983). Transient involvement of the gnal recognition particle and its receptor in the microsomal membrane prior to protein translocation. Cell 35, 677-685.
    • (1983) Cell , vol.35 , pp. 677-685
    • Gilmore, R.1    Blobel, G.2
  • 14
    • 0026466143 scopus 로고
    • A mammalian homologue of Sec61p and SecYp is associated with ribosomes and nascent polypeptides during translocation
    • Görlich, D., Prehn, S., Hartmann, E., Kalies, K.-U., and Rapoport, T.A. (1992). A mammalian homologue 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
  • 15
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the ER membrane
    • Görlich, D., and Rapoport, T.A. (1993). Protein translocation into proteoliposomes reconstituted from purified components of the ER membrane. Cell 75, 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 17
    • 0025762681 scopus 로고
    • Requirements for the membrane insertion of signal-anchor type proteins
    • High, S., Flint, N., and Dobberstein, B. (1991). Requirements for the membrane insertion of signal-anchor type proteins. J. Cell Biol. 113, 25-34.
    • (1991) J. Cell Biol. , vol.113 , pp. 25-34
    • High, S.1    Flint, N.2    Dobberstein, B.3
  • 18
    • 0023665149 scopus 로고
    • A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP binding protein
    • Hwang, Y.-W., and Miller, D.L. (1987). A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP binding protein. J. Biol. Chem. 262, 13081-13085.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13081-13085
    • Hwang, Y.-W.1    Miller, D.L.2
  • 19
    • 0027953913 scopus 로고
    • Binding of ribosomes to the rough endoplasmic reticulum is mediated by the Sec61p-complex
    • Kalies, K.-U., Görlich, D., and Rapoport, T.A. (1994). Binding of ribosomes to the rough endoplasmic reticulum is mediated by the Sec61p-complex. J. Cell Biol. 126, 925-934.
    • (1994) J. Cell Biol. , vol.126 , pp. 925-934
    • Kalies, K.-U.1    Görlich, D.2    Rapoport, T.A.3
  • 20
    • 0026092029 scopus 로고
    • Endoplasmic reticulum translocation intermediates are adjacent to a non-glycosylated 34 kD integral membrane protein
    • Kellaris, K.V., Bowen, S., and Gilmore, R. (1991). Endoplasmic reticulum translocation intermediates are adjacent to a non-glycosylated 34 kD integral membrane protein. J. Cell Biol. 114, 21-33.
    • (1991) J. Cell Biol. , vol.114 , pp. 21-33
    • Kellaris, K.V.1    Bowen, S.2    Gilmore, R.3
  • 21
    • 0005614190 scopus 로고
    • Photocrosslinking of the signal sequence of nascent preprolactin to the 54 kD polypeptide of the signal recognition particle
    • Krieg, U.C., Walter, P., and Johnson, A.E. (1986). Photocrosslinking of the signal sequence of nascent preprolactin to the 54 kD 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
  • 22
    • 0022527444 scopus 로고
    • The signal sequence of nascent preprolactin interacts with the 54 kD polypeptide of the signal recognition particle
    • Kurzchalia, T.V., Wiedmann, M., Girshovich, A.S., Bochkareva, E.S., Bielka, H., and Rapoport, T.A. (1986). The signal sequence of nascent preprolactin interacts with the 54 kD 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
  • 23
    • 0026533588 scopus 로고
    • The methionine rich domain of the 54 kDa subunit of the signal recognition particle is sufficient for the interaction with signal sequences
    • Lütcke, H., High, S., Römisch, K., Ashford, A.J., and Dobberstein, B. (1992). The methionine rich domain of the 54 kDa subunit of the signal recognition particle is sufficient for the interaction with signal sequences. EMBO J. 11, 1543-1551.
    • (1992) EMBO J. , vol.11 , pp. 1543-1551
    • Lütcke, H.1    High, S.2    Römisch, K.3    Ashford, A.J.4    Dobberstein, B.5
  • 24
    • 0027741139 scopus 로고
    • Separate GTP binding and GTPase activating domains of a G alpha subunit
    • Markby, D.W., Onrust, R., and Bourne, H.R. (1993). Separate GTP binding and GTPase activating domains of a G alpha subunit. Science 262, 1895-1901.
    • (1993) Science , vol.262 , pp. 1895-1901
    • Markby, D.W.1    Onrust, R.2    Bourne, H.R.3
  • 25
    • 0027433308 scopus 로고
    • GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
    • Miller, J.D., Wilhelm, H., Gierasch, R., Gilmore, R., and Walter, P. (1993). GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366, 351-354.
    • (1993) Nature , vol.366 , pp. 351-354
    • Miller, J.D.1    Wilhelm, H.2    Gierasch, R.3    Gilmore, R.4    Walter, P.5
  • 26
    • 0028158717 scopus 로고
    • Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor
    • Miller, J.D., Bernstein, H.D., and Walter, P. (1994). Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor. Nature 367, 657-659.
    • (1994) Nature , vol.367 , pp. 657-659
    • Miller, J.D.1    Bernstein, H.D.2    Walter, P.3
  • 27
    • 0028930545 scopus 로고
    • The β subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the a subunit, a peripheral membrane GTPase, to the endoplasmic reticulum
    • Miller, J.D., Tajima, S., Lauffer, L., and Walter, P. (1995). The β subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the a subunit, a peripheral membrane GTPase, to the endoplasmic reticulum. J. Cell Biol. 128, 273-282.
    • (1995) J. Cell Biol. , vol.128 , pp. 273-282
    • Miller, J.D.1    Tajima, S.2    Lauffer, L.3    Walter, P.4
  • 28
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal recognition particle receptor FtsY
    • Montoya, G., Svensson, C., Luirink, J., and Sinning, I. (1997). Crystal structure of the NG domain from the signal recognition particle receptor FtsY. Nature 385, 365-368.
    • (1997) Nature , vol.385 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 29
    • 0029097359 scopus 로고
    • Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
    • Powers, T., and Walter, P. (1995). Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 269, 1422-1424.
    • (1995) Science , vol.269 , pp. 1422-1424
    • Powers, T.1    Walter, P.2
  • 30
    • 0026557511 scopus 로고
    • Protein translocation across the ER requires a functional GTP binding site in the a subunit of the signal recognition particle receptor
    • Rapiejko, P.J., and Gilmore, R. (1992). Protein translocation across the ER requires a functional GTP binding site in the a subunit of the signal recognition particle receptor. J. Cell Biol. 117, 493-503.
    • (1992) J. Cell Biol. , vol.117 , pp. 493-503
    • Rapiejko, P.J.1    Gilmore, R.2
  • 31
    • 0027956144 scopus 로고
    • Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP
    • Rapiejko, P.J., and Gilmore, R. (1994). Signal sequence recognition and targeting of ribosomes to the endoplasmic reticulum by the signal recognition particle do not require GTP. Mol. Biol. Cell 5, 887-897.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 887-897
    • Rapiejko, P.J.1    Gilmore, R.2
  • 32
    • 0024400708 scopus 로고
    • Homology of the 54K protein of signal recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
    • Römisch, K., Webb, J., Herz, J., Prehn, S., Frank, R., Vingron, M., and Dobberstein, B. (1989). Homology of the 54K protein of signal recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains. Nature 340, 478-482.
    • (1989) Nature , vol.340 , pp. 478-482
    • Römisch, K.1    Webb, J.2    Herz, J.3    Prehn, S.4    Frank, R.5    Vingron, M.6    Dobberstein, B.7
  • 33
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S.M., and Blobel, G. (1991). A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 34
    • 0031472242 scopus 로고    scopus 로고
    • The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt, N.D., Newitt, J.A., and Bernstein, H.D. (1997). The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88, 187-196.
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 35
    • 0019849075 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein
    • Walter, P., Ibrahimi, I., and Blobel, G. (1981). Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein. J. Cell Biol. 91, 545-550.
    • (1981) J. Cell Biol. , vol.91 , pp. 545-550
    • Walter, P.1    Ibrahimi, I.2    Blobel, G.3
  • 36
    • 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
  • 37
    • 0031031912 scopus 로고    scopus 로고
    • Synthesis and effect of non-hydrolyzable xanthosine triphosphate derivatives on prenylation of Rab5D136N
    • Yanachkov, I., Pan, J.Y., Wessling-Resnick, M., and Wright, G.E. (1997). Synthesis and effect of non-hydrolyzable xanthosine triphosphate derivatives on prenylation of Rab5D136N. Mol. Pharmacol. 51, 47-51.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 47-51
    • Yanachkov, I.1    Pan, J.Y.2    Wessling-Resnick, M.3    Wright, G.E.4
  • 38
    • 0029072772 scopus 로고
    • An amino-terminal domain containing hydrophobic and hydrophilic sequences binds the signal recognition particle receptor alpha subunit to the beta subunit on the endoplasmic reticulum
    • Young, J.C., Ursini, J., Legate, K.R., Miller, J.D., Walter, P., and Andrews, D.W. (1995). An amino-terminal domain containing hydrophobic and hydrophilic sequences binds the signal recognition particle receptor alpha subunit to the beta subunit on the endoplasmic reticulum. J. Biol. Chem. 70, 15650-15657.
    • (1995) J. Biol. Chem. , vol.70 , pp. 15650-15657
    • Young, J.C.1    Ursini, J.2    Legate, K.R.3    Miller, J.D.4    Walter, P.5    Andrews, D.W.6
  • 39
    • 0025601549 scopus 로고
    • The methionine-rich domain of the 54 kD protein subunit of the signal recognition particle contains an RNA binding site and can be cross-linked to a signal sequence
    • Zopf, D., Bernstein, H.D., Johnson, A.E., and Walter, P. (1990). The methionine-rich domain of the 54 kD protein subunit of the signal recognition particle contains an RNA binding site and can be cross-linked to a signal sequence. EMBO J. 9, 4511-4517.
    • (1990) EMBO J. , vol.9 , pp. 4511-4517
    • Zopf, D.1    Bernstein, H.D.2    Johnson, A.E.3    Walter, P.4


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