메뉴 건너뛰기




Volumn 43, Issue 1, 2004, Pages 107-117

Signal Recognition Particle Alu Domain Occupies a Defined Site at the Ribosomal Subunit Interface upon Signal Sequence Recognition

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CROSSLINKING;

EID: 0346096862     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0353777     Document Type: Article
Times cited : (26)

References (44)
  • 2
    • 0019822645 scopus 로고
    • Transloction of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequence and site specific arrest of chain elongation that is released by microsomal membranes
    • Walter, P., and Blobel, G. (1981) Transloction of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequence and site specific arrest of chain elongation that is released by microsomal membranes, J. Cell. Biol. 91, 557-561.
    • (1981) J. Cell. Biol. , vol.91 , pp. 557-561
    • Walter, P.1    Blobel, G.2
  • 3
    • 0023644552 scopus 로고
    • Signal Recognition Particle Arrest Elongation of Nascent Secretory and Membrane Proteins at Multiple Sites in a Transient Manner
    • Lipp, J., Dobberstein, B., and Haeuptle, M.-T. (1987) Signal Recognition Particle Arrest Elongation of Nascent Secretory and Membrane Proteins at Multiple Sites in a Transient Manner, J. Biol. Chem. 262, 1680-1684.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1680-1684
    • Lipp, J.1    Dobberstein, B.2    Haeuptle, M.-T.3
  • 4
    • 0020413603 scopus 로고
    • Protein Translocation Across the Endoplasmic Reticulum. II. Isolation and characterization of the Signal Recognition Particle Receptor
    • Gilmore, R., Walter, P., and Blobel, G. (1982) Protein Translocation Across the Endoplasmic Reticulum. II. Isolation and characterization of the Signal Recognition Particle Receptor, J. Cell Biol. 95, 470-477.
    • (1982) J. Cell Biol. , vol.95 , pp. 470-477
    • Gilmore, R.1    Walter, P.2    Blobel, G.3
  • 5
    • 0019947629 scopus 로고
    • Secretory protein translocation across membranes - The role of the docking protein
    • Meyer, D. I., Krause, E., and Dobberstein, B. (1982) Secretory protein translocation across membranes - the role of the docking protein, Nature 297, 647-650.
    • (1982) Nature , vol.297 , pp. 647-650
    • Meyer, D.I.1    Krause, E.2    Dobberstein, B.3
  • 6
    • 0030222331 scopus 로고    scopus 로고
    • Approaching the mechanism of protein transport across the ER membrane
    • Rapoport, T. A., Rolls, M. M., and Jungnickel, B. (1996) Approaching the mechanism of protein transport across the ER membrane, Curr. Opin. Cell Biol. 8, 499-504.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 499-504
    • Rapoport, T.A.1    Rolls, M.M.2    Jungnickel, B.3
  • 7
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • Johnson, A. E., and van Waes, M. A. (1999) The translocon: a dynamic gateway at the ER membrane, Annu. Rev. Cell. Dev. Biol. 15, 799-842.
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 799-842
    • Johnson, A.E.1    Van Waes, M.A.2
  • 8
    • 0028930545 scopus 로고
    • The β subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the α subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane
    • 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 α subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane, 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
  • 9
    • 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
  • 10
    • 0023872049 scopus 로고
    • Each of the Activities of Signal Recognition Particle (SRP) Is Contained within a Distinct Domain: Analysis of Biochemical Mutants of SRP
    • Siegel, V., and Walter, P. (1988) Each of the Activities of Signal Recognition Particle (SRP) Is Contained within a Distinct Domain: Analysis of Biochemical Mutants of SRP, Cell 52, 39-49.
    • (1988) Cell , vol.52 , pp. 39-49
    • Siegel, V.1    Walter, P.2
  • 11
    • 0024817509 scopus 로고
    • Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate
    • Wolin, S. L., and Walter, P. (1989) Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate, J. Cell Biol. 109, 2617-2622.
    • (1989) J. Cell Biol. , vol.109 , pp. 2617-2622
    • Wolin, S.L.1    Walter, P.2
  • 12
    • 0030785575 scopus 로고    scopus 로고
    • A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle
    • Thomas, Y., Bui, N., and Strub, K. (1997) A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle, Nucleic Acids Res. 25, 1920-1929.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1920-1929
    • Thomas, Y.1    Bui, N.2    Strub, K.3
  • 13
    • 0034254190 scopus 로고    scopus 로고
    • Elongation arrest is a physiologically important function of signal recognition particle
    • Mason, N., Ciufo, L. F., and Brown, J. D. (2000) Elongation arrest is a physiologically important function of signal recognition particle, EMBO J. 19, 4164-4174.
    • (2000) EMBO J. , vol.19 , pp. 4164-4174
    • Mason, N.1    Ciufo, L.F.2    Brown, J.D.3
  • 14
    • 0022620481 scopus 로고
    • Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact
    • Siegel, V., and Walter, P. (1986) Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact, Nature 320, 81-84.
    • (1986) Nature , vol.320 , pp. 81-84
    • Siegel, V.1    Walter, P.2
  • 15
    • 0023292989 scopus 로고
    • Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking
    • Wiedmann, M., Kurzchalia, T. V., Bielka, H., and Rapoport, T. A. (1987) Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking, J. Cell Biol. 104, 201-208.
    • (1987) J. Cell Biol. , vol.104 , pp. 201-208
    • Wiedmann, M.1    Kurzchalia, T.V.2    Bielka, H.3    Rapoport, T.A.4
  • 16
    • 0023917883 scopus 로고
    • Full-length prepro-α-factor can be translocated across the mammalian microsomal membrane only if translation has not terminated
    • Garcia, P. D., and Walter, P. (1988) Full-length prepro-α-factor can be translocated across the mammalian microsomal membrane only if translation has not terminated, J. Cell Biol. 106, 1043-1048.
    • (1988) J. Cell Biol. , vol.106 , pp. 1043-1048
    • Garcia, P.D.1    Walter, P.2
  • 17
    • 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 (see comments), 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
  • 18
    • 0037162838 scopus 로고    scopus 로고
    • Distinct modes of signal recognition particle interaction with the ribosome
    • Pool, M. R., Stumm, J., Fulga, T. A., Sinning, I., and Dobberstein, B. (2002) Distinct modes of signal recognition particle interaction with the ribosome, Science 297, 1345-1348.
    • (2002) Science , vol.297 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 19
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann, R., Spahn, C. M., Eswar, N., Helmers, J., Penczek, P. A., Sali, A., Frank, J., and Blobel, G. (2001) Architecture of the protein-conducting channel associated with the translating 80S ribosome, Cell 107, 361-372.
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1    Spahn, C.M.2    Eswar, N.3    Helmers, J.4    Penczek, P.A.5    Sali, A.6    Frank, J.7    Blobel, G.8
  • 20
    • 0037406142 scopus 로고    scopus 로고
    • The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome
    • Gu, S. Q., Peske, F., Wieden, H. J., Rodnina, M. V., and Wintermeyer, W. (2003) The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome, RNA 9, 566-573.
    • (2003) RNA , vol.9 , pp. 566-573
    • Gu, S.Q.1    Peske, F.2    Wieden, H.J.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 22
    • 0022423537 scopus 로고
    • The secondary structure of the 7SL RNA in the signal recognition particle: Functional implications
    • Zwieb, C. (1985) The secondary structure of the 7SL RNA in the signal recognition particle: functional implications, Nucleic Acids Res. 13, 6105-6124.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 6105-6124
    • Zwieb, C.1
  • 23
    • 0022827170 scopus 로고
    • Mechanism of Protein Translocation Across the Endoplasmic Reticulum Membrane
    • Walter, P., and Lingappa, V. R. (1986) Mechanism of Protein Translocation Across the Endoplasmic Reticulum Membrane, Annu. Rev. Cell Biol. 2, 499-516.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 499-516
    • Walter, P.1    Lingappa, V.R.2
  • 24
    • 0034626729 scopus 로고    scopus 로고
    • Structure and assembly of the Alu domain of the mammalian signal recognition particle
    • Weichenrieder, O., Wild, K., Strub, K., and Cusack, S. (2000) Structure and assembly of the Alu domain of the mammalian signal recognition particle, Nature 408, 167-173.
    • (2000) Nature , vol.408 , pp. 167-173
    • Weichenrieder, O.1    Wild, K.2    Strub, K.3    Cusack, S.4
  • 25
    • 0030111259 scopus 로고    scopus 로고
    • The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome
    • Powers, T., and Walter, P. (1996) The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome, Curr. Biol. 6, 331-338.
    • (1996) Curr. Biol. , vol.6 , pp. 331-338
    • Powers, T.1    Walter, P.2
  • 26
    • 0031908790 scopus 로고    scopus 로고
    • Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction
    • Neuhof, A., Rolls, M. M., Jungnickel, B., Kalies, K. U., and Rapoport, T. A. (1998) Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction, Mol. Biol. Cell 9, 103-115.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 103-115
    • Neuhof, A.1    Rolls, M.M.2    Jungnickel, B.3    Kalies, K.U.4    Rapoport, T.A.5
  • 27
    • 0029011245 scopus 로고
    • The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs
    • Bovia, F., Fornallaz, M., Leffers, H., and Strub, K. (1995) The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs, Mol. Biol. Cell 6, 471-484.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 471-484
    • Bovia, F.1    Fornallaz, M.2    Leffers, H.3    Strub, K.4
  • 28
    • 0021010426 scopus 로고
    • Signal recognition particle: A ribonucleoprotein required for cotranslational translocation of proteins, isolation, and properties
    • Walter, P., and Blobel, G. (1983) Signal recognition particle: a ribonucleoprotein required for cotranslational translocation of proteins, isolation, and properties, Methods Enzymol. 96, 682-691.
    • (1983) Methods Enzymol. , vol.96 , pp. 682-691
    • Walter, P.1    Blobel, G.2
  • 29
    • 0038719738 scopus 로고    scopus 로고
    • Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens
    • Flanagan, J. J., Chen, J. C., Miao, Y., Shao, Y., Lin, J., Bock, P. E., and Johnson, A. E. (2003) Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens, J. Biol. Chem. 278, 18628-18637.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18628-18637
    • Flanagan, J.J.1    Chen, J.C.2    Miao, Y.3    Shao, Y.4    Lin, J.5    Bock, P.E.6    Johnson, A.E.7
  • 30
    • 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
  • 31
    • 0028874760 scopus 로고
    • A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins
    • Hauser, S., Bacher, G., Dobberstein, B., and Lutcke, H. (1995) A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins, EMBO J. 14, 5485-5493.
    • (1995) EMBO J. , vol.14 , pp. 5485-5493
    • Hauser, S.1    Bacher, G.2    Dobberstein, B.3    Lutcke, H.4
  • 32
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • Thulasiraman, V., Yang, C. F., and Frydman, J. (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment, EMBO J. 18, 85-95.
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 33
    • 0029068214 scopus 로고
    • SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation
    • Ogg, S. C., and Walter, P. (1995) SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation, Cell 81, 1075- 1084.
    • (1995) Cell , vol.81 , pp. 1075-1084
    • Ogg, S.C.1    Walter, P.2
  • 34
    • 0004489150 scopus 로고
    • Structure of the signal recognition particle by electron microscopy
    • Andrews, D. W., Walter, P., and Ottensmeyer, F. P. (1985) Structure of the signal recognition particle by electron microscopy, Proc. Natl. Acad. Sci. U.S.A. 82, 785-789.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 785-789
    • Andrews, D.W.1    Walter, P.2    Ottensmeyer, F.P.3
  • 35
    • 0026079366 scopus 로고
    • Changes in 7SL RNA conformation during the signal recognition particle cycle
    • Andreazzoli, M., and Gerbi, S. A. (1991) Changes in 7SL RNA conformation during the signal recognition particle cycle, EMBO J. 10, 767-777.
    • (1991) EMBO J. , vol.10 , pp. 767-777
    • Andreazzoli, M.1    Gerbi, S.A.2
  • 36
    • 0035051603 scopus 로고    scopus 로고
    • Hierarchical assembly of the Alu domain of the mammalian signal recognition particle
    • Weichenrieder, O., Stehlin, C., Kapp, U., Birse, D. E., Timmins, P. A., Strub, K., and Cusack, S. (2001) Hierarchical assembly of the Alu domain of the mammalian signal recognition particle, RNA 7, 731-740.
    • (2001) RNA , vol.7 , pp. 731-740
    • Weichenrieder, O.1    Stehlin, C.2    Kapp, U.3    Birse, D.E.4    Timmins, P.A.5    Strub, K.6    Cusack, S.7
  • 37
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • Agrawal, R. K., Heagle, A. B., Penczek, P., Grassucci, R. A., and Frank, J. (1999) EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome, Nat. Struct. Biol. 6, 643-647.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 39
    • 0029402642 scopus 로고
    • Structure and evolution of mammalian ribosomal proteins
    • Wool, I. G., Chan, Y. L., and Gluck, A. (1995) Structure and evolution of mammalian ribosomal proteins, Biochem. Cell Biol. 73, 933-947.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 933-947
    • Wool, I.G.1    Chan, Y.L.2    Gluck, A.3
  • 40
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution, Science 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 42
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions
    • Spahn, C. M., Beckmann, R., Eswar, N., Penczek, P. A., Sali, A., Blobel, G., and Frank, J. (2001) Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions, Cell 107, 373-386.
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 43
    • 0020337793 scopus 로고
    • Identification by RNA-protein cross-linking of ribosomal proteins located at the interface between the small and the large subunits of mammalian ribosomes
    • Nygard, O., and Nika, H. (1982) Identification by RNA-protein cross-linking of ribosomal proteins located at the interface between the small and the large subunits of mammalian ribosomes, EMBO J. 1, 357-362.
    • (1982) EMBO J. , vol.1 , pp. 357-362
    • Nygard, O.1    Nika, H.2
  • 44
    • 0022970830 scopus 로고
    • Cross-linking study on protein neighborhoods at the subunit interface of rat liver ribosomes with 2-iminothiolane
    • Uchiumi, T., Kikuchi, M., and Ogata, K. (1986) Cross-linking study on protein neighborhoods at the subunit interface of rat liver ribosomes with 2-iminothiolane, J. Biol. Chem. 261, 9663-9667.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9663-9667
    • Uchiumi, T.1    Kikuchi, M.2    Ogata, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.