메뉴 건너뛰기




Volumn 15, Issue 9, 2008, Pages 916-923

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction

Author keywords

[No Author keywords available]

Indexed keywords

DOCKING PROTEIN; FFH ENZYME; FTSY ENZYME; GUANOSINE TRIPHOSPHATASE; HELICASE; SIGNAL RECOGNITION PARTICLE; UNCLASSIFIED DRUG;

EID: 51349165658     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1467     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 17044419154 scopus 로고    scopus 로고
    • Targeting proteins to membranes: Structure of the signal recognition particle
    • Egea, P.F., Stroud, R.M. & Walter, P. Targeting proteins to membranes: structure of the signal recognition particle. Curr. Opin. Struct. Biol. 15, 213-220 (2005).
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 213-220
    • Egea, P.F.1    Stroud, R.M.2    Walter, P.3
  • 3
    • 0035909810 scopus 로고    scopus 로고
    • Peluso, P., Shan, S.O., Nock, S., Herschlag, D. & Walter, P. Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry 40, 15224-15233 (2001).
    • Peluso, P., Shan, S.O., Nock, S., Herschlag, D. & Walter, P. Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry 40, 15224-15233 (2001).
  • 4
    • 0027433308 scopus 로고
    • GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
    • Miller, J.D., Wilhelm, H., Gierasch, L., Gilmore, R. & Walter, P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366, 351-354 (1993).
    • (1993) Nature , vol.366 , pp. 351-354
    • Miller, J.D.1    Wilhelm, H.2    Gierasch, L.3    Gilmore, R.4    Walter, P.5
  • 5
    • 0025605808 scopus 로고
    • An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle
    • Poritz, M.A. et al. An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science 250, 1111-1117 (1990).
    • (1990) Science , vol.250 , pp. 1111-1117
    • Poritz, M.A.1
  • 6
    • 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. & Walter, P. 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).
    • (1994) Nature , vol.367 , pp. 657-659
    • Miller, J.D.1    Bernstein, H.D.2    Walter, P.3
  • 7
    • 0026794697 scopus 로고    scopus 로고
    • Phillips, G.J. & Silhavy, T.J. The E. coli ffh gene is necessary for viability and efficient protein export. Nature 359, 744-746 (1992).
    • Phillips, G.J. & Silhavy, T.J. The E. coli ffh gene is necessary for viability and efficient protein export. Nature 359, 744-746 (1992).
  • 8
    • 1842506682 scopus 로고    scopus 로고
    • The core Escherichia coli signal recognition particle receptor contains only the N and G domains of FtsY
    • Eitan, A. & Bibi, E. The core Escherichia coli signal recognition particle receptor contains only the N and G domains of FtsY. J. Bacteriol. 186, 2492-2494 (2004).
    • (2004) J. Bacteriol , vol.186 , pp. 2492-2494
    • Eitan, A.1    Bibi, E.2
  • 9
    • 0027288333 scopus 로고
    • Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog
    • Bernstein, H.D., Zopf, D., Freymann, D.M. & Walter, P. Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog. Proc. Natl. Acad. Sci. USA 90, 5229-5233 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5229-5233
    • Bernstein, H.D.1    Zopf, D.2    Freymann, D.M.3    Walter, P.4
  • 10
    • 0030832397 scopus 로고    scopus 로고
    • Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
    • Powers, T. & Walter, P. Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J. 16, 4880-4886 (1997).
    • (1997) EMBO J , vol.16 , pp. 4880-4886
    • Powers, T.1    Walter, P.2
  • 11
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
    • Montoya, G., Svensson, C., Luirink, J. & Sinning, I. Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 385, 365-368 (1997).
    • (1997) Nature , vol.385 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 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. & Walter, P. Structure of the conserved GTPase domain of the signal recognition particle. Nature 385, 361-364 (1997).
    • (1997) Nature , vol.385 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 14
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • Egea, P.F. et al. Substrate twinning activates the signal recognition particle and its receptor. Nature 427, 215-221 (2004).
    • (2004) Nature , vol.427 , pp. 215-221
    • Egea, P.F.1
  • 15
    • 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. & Doudna, J.A. Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287, 1232-1239 (2000).
    • (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
  • 16
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • Keenan, R.J., Freymann, D.M., Walter, P. & Stroud, R.M. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 94, 181-191 (1998).
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 17
    • 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 crosslinked to a signal sequence
    • Zopf, D., Bernstein, H.D., Johnson, A.E. & Walter, P. The methionine-rich domain of the 54 kD protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J. 9, 4511-4517 (1990).
    • (1990) EMBO J , vol.9 , pp. 4511-4517
    • Zopf, D.1    Bernstein, H.D.2    Johnson, A.E.3    Walter, P.4
  • 18
    • 0030657988 scopus 로고    scopus 로고
    • Membrane association of FtsY, the E. coli SRP receptor
    • de Leeuw, E. et al. Membrane association of FtsY, the E. coli SRP receptor. FEBS Lett. 416, 225-229 (1997).
    • (1997) FEBS Lett , vol.416 , pp. 225-229
    • de Leeuw, E.1
  • 19
    • 33748115860 scopus 로고    scopus 로고
    • Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
    • Angelini, S., Boy, D., Schiltz, E. & Koch, H.G. Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites. J. Cell Biol. 174, 715-724 (2006).
    • (2006) J. Cell Biol , vol.174 , pp. 715-724
    • Angelini, S.1    Boy, D.2    Schiltz, E.3    Koch, H.G.4
  • 20
    • 0036682153 scopus 로고    scopus 로고
    • Prediction of signal recognition particle RNA genes
    • Regalia, M., Rosenblad, M.A. & Samuelsson, T. Prediction of signal recognition particle RNA genes. Nucleic Acids Res. 30, 3368-3377 (2002).
    • (2002) Nucleic Acids Res , vol.30 , pp. 3368-3377
    • Regalia, M.1    Rosenblad, M.A.2    Samuelsson, T.3
  • 21
    • 11144351763 scopus 로고    scopus 로고
    • Identification of chloroplast signal recognition particle RNA genes
    • Rosenblad, M.A. & Samuelsson, T. Identification of chloroplast signal recognition particle RNA genes. Plant Cell Physiol. 45, 1633-1639 (2004).
    • (2004) Plant Cell Physiol , vol.45 , pp. 1633-1639
    • Rosenblad, M.A.1    Samuelsson, T.2
  • 22
    • 0021645935 scopus 로고
    • The 4.5 S RNA gene of Escherichia coli is essential for cell growth
    • Brown, S. & Fournier, M.J. The 4.5 S RNA gene of Escherichia coli is essential for cell growth. J. Mol. Biol. 178, 533-550 (1984).
    • (1984) J. Mol. Biol , vol.178 , pp. 533-550
    • Brown, S.1    Fournier, M.J.2
  • 23
    • 0034596007 scopus 로고    scopus 로고
    • Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor
    • Peluso, P. et al. Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor. Science 288, 1640-1643 (2000).
    • (2000) Science , vol.288 , pp. 1640-1643
    • Peluso, P.1
  • 24
    • 34347399347 scopus 로고    scopus 로고
    • The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting
    • Bradshaw, N. & Walter, P. The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting. Mol. Biol. Cell 18, 2728-2734 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2728-2734
    • Bradshaw, N.1    Walter, P.2
  • 25
    • 36148931107 scopus 로고    scopus 로고
    • X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates
    • Reyes, C.L., Rutenber, E., Walter, P. & Stroud, R.M. X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates. PLoS ONE 2, e607 (2007).
    • (2007) PLoS ONE , vol.2
    • Reyes, C.L.1    Rutenber, E.2    Walter, P.3    Stroud, R.M.4
  • 26
    • 33947320768 scopus 로고    scopus 로고
    • Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY
    • Gawronski-Salerno, J. & Freymann, D. M. Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY. J. Struct. Biol. 158, 122-128 (2006).
    • (2006) J. Struct. Biol , vol.158 , pp. 122-128
    • Gawronski-Salerno, J.1    Freymann, D.M.2
  • 27
    • 33745644462 scopus 로고    scopus 로고
    • 4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site
    • 4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site. J. Mol. Biol. 360, 631-643 (2006).
    • (2006) J. Mol. Biol , vol.360 , pp. 631-643
    • Focia, P.J.1    Gawronski-Salerno, J.2    Coon, J.S.V.3    Freymann, D.M.4
  • 28
    • 0037140924 scopus 로고    scopus 로고
    • Conformational change of the N domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY
    • Shepotinovskaya, I.V. & Freymann, D.M. Conformational change of the N domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY. Biochim. Biophys. Acta 1597, 107-114 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 107-114
    • Shepotinovskaya, I.V.1    Freymann, D.M.2
  • 29
    • 36549025508 scopus 로고    scopus 로고
    • Structure of the chloroplast signal recognition particle (SRP) receptor: Domain arrangement modulates SRP-receptor interaction
    • Chandrasekar, S., Chartron, J., Jaru-Ampornpan, P. & Shan, S.O. Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction. J. Mol. Biol. 375, 425-436 (2008).
    • (2008) J. Mol. Biol , vol.375 , pp. 425-436
    • Chandrasekar, S.1    Chartron, J.2    Jaru-Ampornpan, P.3    Shan, S.O.4
  • 30
    • 0034723143 scopus 로고    scopus 로고
    • Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP
    • Jagath, J.R., Rodnina, M.V. & Wintermeyer, W. Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP. J. Mol. Biol. 295, 745-753 (2000).
    • (2000) J. Mol. Biol , vol.295 , pp. 745-753
    • Jagath, J.R.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 31
    • 0029856954 scopus 로고    scopus 로고
    • NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP)
    • Schmitz, U. et al. NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP). RNA 2, 1213-1227 (1996).
    • (1996) RNA , vol.2 , pp. 1213-1227
    • Schmitz, U.1
  • 32
    • 17644425296 scopus 로고    scopus 로고
    • Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor
    • Shan, S.O. & Walter, P. Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor. Biochemistry 44, 6214-6222 (2005).
    • (2005) Biochemistry , vol.44 , pp. 6214-6222
    • Shan, S.O.1    Walter, P.2
  • 33
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers, R. & Kay, L.E. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445, 618-622 (2007).
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 34
    • 33847016483 scopus 로고    scopus 로고
    • X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases
    • Gawronski-Salerno, J., Coon, J.S., V., Focia, P.J. & Freymann, D.M. X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases. Proteins 66, 984-995 (2007).
    • (2007) Proteins , vol.66 , pp. 984-995
    • Gawronski-Salerno, J.1    Coon, J.S.V.2    Focia, P.J.3    Freymann, D.M.4
  • 35
    • 29844458697 scopus 로고    scopus 로고
    • Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY
    • Gariani, T., Samuelsson, T. & Sauer-Eriksson, A.E. Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY. J. Struct. Biol. 153, 85-96 (2006).
    • (2006) J. Struct. Biol , vol.153 , pp. 85-96
    • Gariani, T.1    Samuelsson, T.2    Sauer-Eriksson, A.E.3
  • 36
    • 8844253060 scopus 로고    scopus 로고
    • Mechanism of association and reciprocal activation of two GTPases
    • Shan, S.O., Stroud, R.M. & Walter, P. Mechanism of association and reciprocal activation of two GTPases. PLoS Biol. 2, e320 (2004).
    • (2004) PLoS Biol , vol.2
    • Shan, S.O.1    Stroud, R.M.2    Walter, P.3
  • 37
    • 0035803599 scopus 로고    scopus 로고
    • Evidence for a novel GTPase priming step in the SRP protein targeting pathway
    • Lu, Y. et al. Evidence for a novel GTPase priming step in the SRP protein targeting pathway. EMBO J. 20, 6724-6734 (2001).
    • (2001) EMBO J , vol.20 , pp. 6724-6734
    • Lu, Y.1
  • 38
    • 9344221072 scopus 로고    scopus 로고
    • Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry
    • Chu, F. et al. Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry. Proc. Natl. Acad. Sci. USA 101, 16454-16459 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16454-16459
    • Chu, F.1
  • 39
    • 36148937889 scopus 로고    scopus 로고
    • Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix
    • Parlitz, R. et al. Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. J. Biol. Chem. 282, 32176-32184 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 32176-32184
    • Parlitz, R.1
  • 40
    • 36049049032 scopus 로고    scopus 로고
    • Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY
    • Bahari, L. et al. Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY. J. Biol. Chem. 282, 32168-32175 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 32168-32175
    • Bahari, L.1
  • 41
    • 0037354160 scopus 로고    scopus 로고
    • A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes
    • Gross, J.D., Gelev, V.M. & Wagner, G. A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes. J. Biomol. NMR 25, 235-242 (2003).
    • (2003) J. Biomol. NMR , vol.25 , pp. 235-242
    • Gross, J.D.1    Gelev, V.M.2    Wagner, G.3
  • 42
    • 0032898682 scopus 로고    scopus 로고
    • A robust and costeffective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins
    • Goto, N.K., Gardner, K.H., Mueller, G.A., Willis, R.C. & Kay, L.E. A robust and costeffective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins. J. Biomol. NMR 13, 369-374 (1999).
    • (1999) J. Biomol. NMR , vol.13 , pp. 369-374
    • Goto, N.K.1    Gardner, K.H.2    Mueller, G.A.3    Willis, R.C.4    Kay, L.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.