메뉴 건너뛰기




Volumn 30, Issue 19, 2002, Pages 4166-4175

Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; PROTEIN SUBUNIT; RIBONUCLEOPROTEIN; RNA; SIGNAL RECOGNITION PARTICLE; SODIUM CHLORIDE;

EID: 0036799450     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkf548     Document Type: Review
Times cited : (32)

References (42)
  • 1
    • 85041115207 scopus 로고    scopus 로고
    • New prospects in studying the bacterial signal recognition particle pathway
    • Herskovits,A.A., Bochkareva,E.S. and Bibi,E. (2000) New prospects in studying the bacterial signal recognition particle pathway. Mol. Microbiol., 38, 927-939.
    • (2000) Mol. Microbiol , vol.38 , pp. 927-939
    • Herskovits, A.A.1    Bochkareva, E.S.2    Bibi, E.3
  • 2
    • 0035283319 scopus 로고    scopus 로고
    • The signal recognition particle of archaea
    • Eichler,J. and Moll,R. (2001) The signal recognition particle of archaea. Trends Microbiol., 9, 130-136.
    • (2001) Trends Microbiol , vol.9 , pp. 130-136
    • Eichler, J.1    Moll, R.2
  • 4
    • 0028964746 scopus 로고
    • Signal recognition particle (SRP), a ubiquitous initiator of protein translocation
    • Lütcke,H. (1995) Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur. J. Biochem., 228, 531-550.
    • (1995) Eur. J. Biochem , vol.228 , pp. 531-550
    • Lütcke, H.1
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0034254190 scopus 로고    scopus 로고
    • Elongation arrest is a physiologically important function of signal recognition particle
    • Mason,N., CiufoL.F. and Brown,N. (2000) Elongation arrest is a physiologically important function of signal recognition particle. EMBO J., 15, 4164-4174.
    • (2000) EMBO J , vol.15 , pp. 4164-4174
    • Mason, N.1    Ciufo, L.F.2    Brown, N.3
  • 9
    • 0032924499 scopus 로고    scopus 로고
    • Expression, purification, and crystallography of the conserved methionine-rich domain of human signal recognition particle 54 kDa protein
    • Gowda,K., Clemons,W.M., Zwieb,C. and Black,S.D. (1999) Expression, purification, and crystallography of the conserved methionine-rich domain of human signal recognition particle 54 kDa protein. Protein Sci., 8, 1144-1151.
    • (1999) Protein Sci , vol.8 , pp. 1144-1151
    • Gowda, K.1    Clemons, W.M.2    Zwieb, C.3    Black, S.D.4
  • 10
    • 0029072772 scopus 로고
    • An amino-terminal-domain containing hydrophobic and hydrophilic sequences binds the signal recognition, particle receptor α subunit to the β subunit on the endoplasmic reticulum membrane
    • 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 α subunit to the β subunit on the endoplasmic reticulum membrane. J. Biol. Chem., 270, 15650-15657.
    • (1995) J. Biol. Chem , vol.270 , 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
  • 11
    • 0033531944 scopus 로고    scopus 로고
    • Bacillus subtilis histone-like protein, HBsu, is an integral component of a SRP-like particle that can bind the Alu domain of small cytoplasmic RNA
    • Nakamura,K., Yahagi,S., Yamazaki,T. and Yamane,K. (1999) Bacillus subtilis histone-like protein, HBsu, is an integral component of a SRP-like particle that can bind the Alu domain of small cytoplasmic RNA. J. Biol. Chem., 274, 13569-13576.
    • (1999) J. Biol. Chem , vol.274 , pp. 13569-13576
    • Nakamura, K.1    Yahagi, S.2    Yamazaki, T.3    Yamane, K.4
  • 12
    • 0031020515 scopus 로고    scopus 로고
    • Fts Y the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins
    • Seluanov,A. and Bibi,E. (1997) Fts Y, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins. J. Biol. Chem., 272, 2053-2055.
    • (1997) J. Biol. Chem , vol.272 , pp. 2053-2055
    • Seluanov, A.1    Bibi, E.2
  • 13
    • 0031472242 scopus 로고
    • The E. coli signal recogition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt,N.D, Newitt,J.A. and Bernstein,H.D. (1977) The E. coli signal recogition particle is required for the insertion of a subset of inner membrane proteins. Cell, 88, 187-196.
    • (1977) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 14
    • 0028876220 scopus 로고
    • The functional integration of a polytopic membrane protein of Escherichia coli is dependent on the bacterial signal-recognition particle
    • MacFarlane,J. and Muller,M. (1995) The functional integration of a polytopic membrane protein of Escherichia coli is dependent on the bacterial signal-recognition particle. Eur. J. Biochem., 233, 766-771.
    • (1995) Eur. J. Biochem , vol.233 , pp. 766-771
    • MacFarlane, J.1    Muller, M.2
  • 15
    • 0002933789 scopus 로고    scopus 로고
    • Getting on target: The archaeal signal recognition particle
    • Zwieb,C. and Eichler,J. (2001) Getting on target: the archaeal signal recognition particle. Archaea, 1, 27-34.
    • (2001) Archaea , vol.1 , pp. 27-34
    • Zwieb, C.1    Eichler, J.2
  • 16
    • 0034654251 scopus 로고    scopus 로고
    • Assembly of archaeal signal recognition particle from recombinant components
    • Bhuiyan,S.H., Gowda, K., Hotokezaka,H. and Zwieb,C. (2000) Assembly of archaeal signal recognition particle from recombinant components Nucleic Acids Res., 15, 1365-1373.
    • (2000) Nucleic Acids Res , vol.15 , pp. 1365-1373
    • Bhuiyan, S.H.1    Gowda, K.2    Hotokezaka, H.3    Zwieb, C.4
  • 17
    • 0035798197 scopus 로고    scopus 로고
    • An archael protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA
    • Maeshima,H., Okuno,E., Aimi,T., Morinaga,T. and Itoh,P. (2000) An archael protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA. FEBS Lett., 507, 336-340.
    • (2000) FEBS Lett , vol.507 , pp. 336-340
    • Maeshima, H.1    Okuno, E.2    Aimi, T.3    Morinaga, T.4    Itoh, P.5
  • 18
    • 0037071839 scopus 로고    scopus 로고
    • Structure of the SRP19 RNA complex and implications for signal recognition particle assembly
    • Hainzl,T., Huang,S. and Sauer-Eriksson,A.E. (2002) Structure of the SRP19 RNA complex and implications for signal recognition particle assembly. Nature, 417, 767-771.
    • (2002) Nature , vol.417 , pp. 767-771
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 19
    • 0036289536 scopus 로고    scopus 로고
    • Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle
    • Oubridge, C., Kuglstatter,A., Jovine,L. and Nagai,K. (2002) Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle. Mol. Cell, 9, 1251-1261.
    • (2002) Mol. Cell , vol.9 , pp. 1251-1261
    • Oubridge, C.1    Kuglstatter, A.2    Jovine, L.3    Nagai, K.4
  • 20
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • Madern,D., Ebel,C. and Zaccai,G. (2000) Halophilic adaptation of enzymes. Extremophiles, 4, 91-98.
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 21
    • 0033152499 scopus 로고    scopus 로고
    • Thermophilic and halophilic extremophiles
    • Madigan,M.T. and Oren,A. (1999) Thermophilic and halophilic extremophiles. Curr. Opin. Microbiol., 2, 265-269.
    • (1999) Curr. Opin. Microbiol , vol.2 , pp. 265-269
    • Madigan, M.T.1    Oren, A.2
  • 22
    • 0022003836 scopus 로고
    • Genetic transfer in Halobacterium volcanii
    • Mevarech,M. and Werczberger,R. (1985) Genetic transfer in Halobacterium volcanii. J. Bacteriol., 162, 461-462.
    • (1985) J. Bacteriol , vol.162 , pp. 461-462
    • Mevarech, M.1    Werczberger, R.2
  • 23
    • 0025765510 scopus 로고
    • Interaction of protein SRP19 with signal recognition particle RNA lacking individual RNA helices
    • Zwieb,C. (1991) Interaction of protein SRP19 with signal recognition particle RNA lacking individual RNA helices. Nucleic Acids Res., 19, 2955-2960.
    • (1991) Nucleic Acids Res , vol.19 , pp. 2955-2960
    • Zwieb, C.1
  • 24
    • 0000680161 scopus 로고
    • Amplification of specific DNA sequences correlates with resistance of the archaebacterium Halobacterium volcanii to the dihydrofolate reductase inhibitors trimethoprim and methotrexate
    • Rosenshine,I., Zusman,T., Werczberger,R. and Mevarech,M. (1987) Amplification of specific DNA sequences correlates with resistance of the archaebacterium Halobacterium volcanii to the dihydrofolate reductase inhibitors trimethoprim and methotrexate. Mol. Gen. Genet., 208, 518-522.
    • (1987) Mol. Gen. Genet , vol.208 , pp. 518-522
    • Rosenshine, I.1    Zusman, T.2    Werczberger, R.3    Mevarech, M.4
  • 25
    • 0025981510 scopus 로고
    • SRP-RNA sequence alignment and secondary structure
    • Larsen,N. and Zwieb,C. (1991) SRP-RNA sequence alignment and secondary structure. Nucleic Acids Res., 19, 209-215.
    • (1991) Nucleic Acids Res , vol.19 , pp. 209-215
    • Larsen, N.1    Zwieb, C.2
  • 27
    • 0028303640 scopus 로고
    • Molecular evolution of SRP cycle components: Functional implications
    • Althoff,S., Selinger,D. and Wise,J.A. (1994) Molecular evolution of SRP cycle components: functional implications. Nucleic Acids Res., 22, 1933-1947.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1933-1947
    • Althoff, S.1    Selinger, D.2    Wise, J.A.3
  • 28
    • 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
  • 29
    • 0036274413 scopus 로고    scopus 로고
    • In vivo analysis of an essential archaeal signal recognition particle in its native host
    • Rose,W. and Pohlschroder,M. (2002) In vivo analysis of an essential archaeal signal recognition particle in its native host. J. Bacteriol., 184, 3260-3267.
    • (2002) J. Bacteriol , vol.184 , pp. 3260-3267
    • Rose, W.1    Pohlschroder, M.2
  • 30
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein,H.D., Poritz,M.A., Strub,K., Hoben,P.J., Brenner,S. and Walter,P. (1989) Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. 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
  • 31
    • 0024400708 scopus 로고
    • Homology of 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 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
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • Batey,R.T., Rambo,R.P., Lucast,L., Rha,B., and Doudna,J.A. (2000) Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science, 287, 1232-1239.
    • (2000) Science , vol.287 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.A.5
  • 34
    • 0000959078 scopus 로고
    • Solute concentrations within cells of halophilic and non-halophilic bacteria
    • Christian,J.H.B. and Waltho,J.A. (1962) Solute concentrations within cells of halophilic and non-halophilic bacteria. Biochim. Biophys. Acta, 65, 506-508.
    • (1962) Biochim. Biophys. Acta , vol.65 , pp. 506-508
    • Christian, J.H.B.1    Waltho, J.A.2
  • 35
    • 0034711041 scopus 로고    scopus 로고
    • Role of SRP19 in assembly of the Archaeologlobus fulgidus signal recognition particle
    • Diener,J.L. and Wilson,C. (2000) Role of SRP19 in assembly of the Archaeologlobus fulgidus signal recognition particle. Biochemistry, 39, 12862-12874.
    • (2000) Biochemistry , vol.39 , pp. 12862-12874
    • Diener, J.L.1    Wilson, C.2
  • 36
    • 0036290864 scopus 로고    scopus 로고
    • Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle
    • Pakhomova,O.N., Deep,S., Huang,Q., Zwieb,C. and Hinck,A.P. (2002) Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle. J. Mol. Biol., 317 145-158.
    • (2002) J. Mol. Biol , vol.317 , pp. 145-158
    • Pakhomova, O.N.1    Deep, S.2    Huang, Q.3    Zwieb, C.4    Hinck, A.P.5
  • 37
    • 0035913989 scopus 로고    scopus 로고
    • Crystal structure of an early protein-RNA assembly complex of the signal recognition particle
    • Wild,K., Sinning,L. and Cusack,S. (2001) Crystal structure of an early protein-RNA assembly complex of the signal recognition particle Science, 294, 598-601.
    • (2001) Science , vol.294 , pp. 598-601
    • Wild, K.1    Sinning, L.2    Cusack, S.3
  • 39
    • 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 Steiz,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    Steiz, T.A.5
  • 40
    • 0024993267 scopus 로고
    • In vitro reassembly of active large ribosomal subunits of the halophilic archaebacterium Haloferazx mediterranei
    • Sanchez,M.E., Urena,D., Amils,R. and Londei P. (1990) In vitro reassembly of active large ribosomal subunits of the halophilic archaebacterium Haloferazx mediterranei. Biochemistry, 29, 9256-9261.
    • (1990) Biochemistry , vol.29 , pp. 9256-9261
    • Sanchez, M.E.1    Urena, D.2    Amils, R.3    Londei, P.4
  • 42
    • 0035474359 scopus 로고    scopus 로고
    • Large-scale preparation and characterization of inverted membrane vesicles from the halophilic archaeon Haloferax volcanii
    • Ring,G. and Eichler,J. (2001) Large-scale preparation and characterization of inverted membrane vesicles from the halophilic archaeon Haloferax volcanii. J Membr. Biol., 183, 195-204.
    • (2001) J. Membr. Biol , vol.183 , pp. 195-204
    • Ring, G.1    Eichler, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.