메뉴 건너뛰기




Volumn 24, Issue 2, 2013, Pages 63-73

Fingerloop activates cargo delivery and unloading during cotranslational protein targeting

Author keywords

[No Author keywords available]

Indexed keywords

DOCKING PROTEIN; GUANOSINE TRIPHOSPHATASE; SIGNAL RECOGNITION PARTICLE;

EID: 84872339013     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-06-0434     Document Type: Article
Times cited : (11)

References (50)
  • 1
    • 79951826865 scopus 로고    scopus 로고
    • The crystal structure of the signal recognition particle in complex with its receptor
    • Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, Doudna JA, Ban N (2011). The crystal structure of the signal recognition particle in complex with its receptor. Science 331, 881-886.
    • (2011) Science , vol.331 , pp. 881-886
    • Ataide, S.F.1    Schmitz, N.2    Shen, K.3    Ke, A.4    Shan, S.O.5    Doudna, J.A.6    Ban, N.7
  • 2
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • DOI 10.1126/science.287.5456.1232
    • Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA (2000). Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287, 1232-1239. (Pubitemid 30112139)
    • (2000) Science , vol.287 , Issue.5456 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.A.5
  • 3
    • 0035896023 scopus 로고    scopus 로고
    • Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle
    • DOI 10.1006/jmbi.2000.4454
    • Batey RT, Sagar MB, Doudna JA (2001). Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle. J Mol Biol 307, 229-246. (Pubitemid 33029978)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.1 , pp. 229-246
    • Batey, R.T.1    Sagar, M.B.2    Doudna, J.A.3
  • 4
    • 0032497570 scopus 로고    scopus 로고
    • Protein targeting: Getting into the groove
    • Bernstein HD (1998). Protein targeting: getting into the groove. Curr Biol 8, R715-R718.
    • (1998) Curr Biol , vol.8
    • Bernstein, H.D.1
  • 5
    • 5444242520 scopus 로고    scopus 로고
    • Bacterial expression system with tightly regulated gene expression and plasmid copy number
    • DOI 10.1016/j.gene.2004.06.012, PII S0378111904003361
    • Bowers LM, Lapoint K, Anthony L, Pluciennik A, Filutowicz M (2004). Bacterial expression system with tightly regulated gene expression and plasmid copy number. Gene 340, 11-18. (Pubitemid 39360228)
    • (2004) Gene , vol.340 , Issue.1 , pp. 11-18
    • Bowers, L.M.1    Lapoint, K.2    Anthony, L.3    Pluciennik, A.4    Filutowicz, M.5
  • 6
    • 58149264965 scopus 로고    scopus 로고
    • Signal sequences activate the catalytic switch of SRP RNA
    • Bradshaw N, Neher SB, Booth DS, Walter P (2009). Signal sequences activate the catalytic switch of SRP RNA. Science 323, 127-130.
    • (2009) Science , vol.323 , pp. 127-130
    • Bradshaw, N.1    Neher, S.B.2    Booth, D.S.3    Walter, P.4
  • 7
    • 34347399347 scopus 로고    scopus 로고
    • The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting
    • DOI 10.1091/mbc.E07-02-0117
    • Bradshaw N, Walter P (2007). The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting. Mol Biol Cell 18, 2728-2734. (Pubitemid 47025737)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.7 , pp. 2728-2734
    • Bradshaw, N.1    Walter, P.2
  • 8
    • 0035377197 scopus 로고    scopus 로고
    • The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle
    • Cleverley RM, Zheng N, Gierasch LM (2001). The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle. J Biol Chem 276, 19327-19331.
    • (2001) J Biol Chem , vol.276 , pp. 19327-19331
    • Cleverley, R.M.1    Zheng, N.2    Gierasch, L.M.3
  • 10
    • 33747333128 scopus 로고    scopus 로고
    • A set of recombineering plasmids for gram-negative bacteria
    • DOI 10.1016/j.gene.2006.04.018, PII S0378111906002927
    • Datta S, Constantino N, Court DL (2006). A set of recombineering plasmids for gram-negative bacteria. Gene 379, 109-115. (Pubitemid 44247330)
    • (2006) Gene , vol.379 , Issue.1-2 , pp. 109-115
    • Datta, S.1    Costantino, N.2    Court, D.L.3
  • 11
    • 3943099373 scopus 로고    scopus 로고
    • Structural insights into the signal recognition particle
    • DOI 10.1146/annurev.biochem.73.011303.074048
    • Doudna JA, Batey RT (2004). Structural insights into the signal recognition particle. Annu Rev Biochem 73, 539-557. (Pubitemid 39050379)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 539-557
    • Doudna, J.A.1    Batey, R.T.2
  • 12
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • DOI 10.1038/nature02250
    • Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM (2004). Substrate twinning activates the signal recognition particle and its receptor. Nature 427, 215-221. (Pubitemid 38112032)
    • (2004) Nature , vol.427 , Issue.6971 , pp. 215-221
    • Egea, P.F.1    Shan, S.-O.2    Napetschnig, J.3    Savage, D.F.4    Walter, P.5    Stroud, R.M.6
  • 13
    • 78650974443 scopus 로고    scopus 로고
    • Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor
    • Estrozi LF, Boehringer D, Shan SO, Ban N, Schaffitzel C (2011). Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nat Struct Mol Biol 18, 88-90.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 88-90
    • Estrozi, L.F.1    Boehringer, D.2    Shan, S.O.3    Ban, N.4    Schaffitzel, C.5
  • 14
    • 0346373753 scopus 로고    scopus 로고
    • Heterodimeric GTPase Core of the SRP Targeting Complex
    • DOI 10.1126/science.1090827
    • Focia PJ, Shepotinovskaya IV, Seidler JA, Freymann DM (2004). Heterodimeric GTPase core of the SRP targeting complex. Science 303, 373-377. (Pubitemid 38095777)
    • (2004) Science , vol.303 , Issue.5656 , pp. 373-377
    • Focia, P.J.1    Shepotinovskaya, I.V.2    Seidler, J.A.3    Freymann, D.M.4
  • 15
    • 0031017523 scopus 로고    scopus 로고
    • Structure of the conserved GTPase domain of the signal recognition particle
    • DOI 10.1038/385361a0
    • Freymann DM, Keenan RJ, Stroud RM, Walter P (1997). Structure of the conserved GTPase domain of the signal recognition particle. Nature 385, 361-364. (Pubitemid 27053109)
    • (1997) Nature , vol.385 , Issue.6614 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 16
    • 0020357598 scopus 로고
    • Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
    • DOI 10.1083/jcb.95.2.463
    • Gilmore R, Blobel G, Walter P (1982a). Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J Cell Biol 95, 463-469. (Pubitemid 13215861)
    • (1982) Journal of Cell Biology , vol.95 , Issue.2 I , pp. 463-469
    • Gilmore, R.1    Blobel, G.2    Walter, P.3
  • 17
    • 0020413603 scopus 로고
    • Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
    • DOI 10.1083/jcb.95.2.470
    • Gilmore R, Walter P, Blobel G (1982b). Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J Cell Biol 95, 470-477. (Pubitemid 13215862)
    • (1982) Journal of Cell Biology , vol.95 , Issue.2 I , pp. 470-477
    • Gilmore, R.1    Walter, P.2    Blobel, G.3
  • 19
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • DOI 10.1038/nature02342
    • Halic M, Becker T, Pool MR, Spahn CM, Grassucci RA, Frank J, Beckmann R (2004). Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427, 808-814. (Pubitemid 38297736)
    • (2004) Nature , vol.427 , Issue.6977 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.T.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 20
    • 13844266603 scopus 로고    scopus 로고
    • The signal recognition particle and its interactions during protein targeting
    • DOI 10.1016/j.sbi.2005.01.013
    • Halic M, Beckmann R (2005). The signal recognition particle and its interactions during protein targeting. Curr Opin Struct Biol 15, 116-125. (Pubitemid 40249518)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.1 SPEC. ISS. , pp. 116-125
    • Halic, M.1    Beckmann, R.2
  • 21
    • 33751325296 scopus 로고    scopus 로고
    • Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    • DOI 10.1038/nature05326, PII NATURE05326
    • Halic M, Blau M, Becker T, Mielke T, Pool MR, Wild K, Sinning I, Beckmann R (2006). Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature 444, 507-511. (Pubitemid 44809070)
    • (2006) Nature , vol.444 , Issue.7118 , pp. 507-511
    • Halic, M.1    Blau, M.2    Becker, T.3    Mielke, T.4    Pool, M.R.5    Wild, K.6    Sinning, I.7    Beckmann, R.8
  • 24
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • DOI 10.1016/S0092-8674(00)81418-X
    • Keenan RJ, Freymann DM, Walter P, Stroud RM (1998). Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 94, 181-191. (Pubitemid 28348006)
    • (1998) Cell , vol.94 , Issue.2 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 25
    • 0038121152 scopus 로고    scopus 로고
    • Signal recognition particle-dependent protein targeting, universal to all kingdoms of life
    • Koch HG, Moser M, Muller M (2003). Signal recognition particle-dependent protein targeting, universal to all kingdoms of life. Rev Physiol Biochem Pharmacol 146, 55-94.
    • (2003) Rev Physiol Biochem Pharmacol , vol.146 , pp. 55-94
    • Koch, H.G.1    Moser, M.2    Muller, M.3
  • 26
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
    • DOI 10.1038/385365a0
    • Montoya G, Svensson C, Luirink J, Sinning I (1997). Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 385, 365-368. (Pubitemid 27053110)
    • (1997) Nature , vol.385 , Issue.6614 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 28
    • 0034596007 scopus 로고    scopus 로고
    • Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor
    • DOI 10.1126/science.288.5471.1640
    • Peluso P, Herschlag D, Nock S, Freymann DM, Johnson AE, Walter P (2000). Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor. Science 288, 1640-1643. (Pubitemid 30387429)
    • (2000) Science , vol.288 , Issue.5471 , pp. 1640-1643
    • Peluso, P.1    Herschlag, D.2    Nock, S.3    Freymann, D.M.4    Johnson, A.E.5    Walter, P.6
  • 29
    • 0035909810 scopus 로고    scopus 로고
    • Role of SRP RNA in the GTPase cycles of Ffh and FtsY
    • DOI 10.1021/bi011639y
    • Peluso P, Shan SO, Nock S, Herschlag D, Walter P (2001). Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry 40, 15224-15233. (Pubitemid 33151937)
    • (2001) Biochemistry , vol.40 , Issue.50 , pp. 15224-15233
    • Peluso, P.1    Shan, S.-O.2    Nock, S.3    Herschlag, D.4    Walter, P.5
  • 30
    • 57349129334 scopus 로고    scopus 로고
    • Characterization of conserved bases in 4.5S RNA of Escherichia coli by construction of new F2 factors
    • Peterson JM, Phillips GJ (2008). Characterization of conserved bases in 4.5S RNA of Escherichia coli by construction of new F2 factors. J Bacteriol 190, 7709-7718.
    • (2008) J Bacteriol , vol.190 , pp. 7709-7718
    • Peterson, J.M.1    Phillips, G.J.2
  • 31
    • 0032928472 scopus 로고    scopus 로고
    • New cloning vectors with temperature sensitive replication
    • Phillips GJ (1999). New cloning vectors with temperature sensitive replication. Plasmid 41, 78-81.
    • (1999) Plasmid , vol.41 , pp. 78-81
    • Phillips, G.J.1
  • 32
    • 0026794697 scopus 로고
    • The E. coli ffh gene is necessary for viability and efficient protein export
    • Phillips GJ, Silhavy TJ (1992). The E. coli ffh gene is necessary for viability and efficient protein export. Nature 359, 744-746.
    • (1992) Nature , vol.359 , pp. 744-746
    • Phillips, G.J.1    Silhavy, T.J.2
  • 33
    • 0037162838 scopus 로고    scopus 로고
    • Distinct modes of signal recognition particle interaction with the ribosome
    • DOI 10.1126/science.1072366
    • Pool MR, Stumm J, Fulga TA, Sinning I, Dobberstein B (2002). Distinct modes of signal recognition particle interaction with the ribosome. Science 297, 1345-1348. (Pubitemid 34913172)
    • (2002) Science , vol.297 , Issue.5585 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 34
    • 0030832397 scopus 로고    scopus 로고
    • Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
    • DOI 10.1093/emboj/16.16.4880
    • Powers T, Walter P (1997). Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J 16, 4880-4886. (Pubitemid 27348397)
    • (1997) EMBO Journal , vol.16 , Issue.16 , pp. 4880-4886
    • Powers, T.1    Walter, P.2
  • 36
    • 80053079082 scopus 로고    scopus 로고
    • Site-specific fluorescent labeling of nascent proteins on the translating ribosome
    • Saraogi I, Zhang D, Chandrasekaran S, Shan SO (2011). Site-specific fluorescent labeling of nascent proteins on the translating ribosome. J Am Chem Soc 133, 14936-14939.
    • (2011) J Am Chem Soc , vol.133 , pp. 14936-14939
    • Saraogi, I.1    Zhang, D.2    Chandrasekaran, S.3    Shan, S.O.4
  • 37
    • 34248583785 scopus 로고    scopus 로고
    • Generation of ribosome nascent chain complexes for structural and functional studies
    • DOI 10.1016/j.jsb.2007.01.005, PII S1047847707000275
    • Schaffitzel C, Ban N (2007). Generation of ribosome nascent chain complexes for structural and functional studies. J Struct Biol 158, 463-471. (Pubitemid 46764575)
    • (2007) Journal of Structural Biology , vol.158 , Issue.3 , pp. 463-471
    • Schaffitzel, C.1    Ban, N.2
  • 38
    • 33751325833 scopus 로고    scopus 로고
    • Structure of the E. coli signal recognition particle bound to a translating ribosome
    • DOI 10.1038/nature05182, PII NATURE05182
    • Schaffitzel C, Oswald M, Berger I, Ishikawa T, Abrahams JP, Koerten HK, Koning RI, Ban N (2006). Structure of the E. coli signal recognition particle bound to a translating ribosome. Nature 444, 503-506. (Pubitemid 44809069)
    • (2006) Nature , vol.444 , Issue.7118 , pp. 503-506
    • Schaffitzel, C.1    Oswald, M.2    Berger, I.3    Ishikawa, T.4    Abrahams, J.P.5    Koerten, H.K.6    Koning, R.I.7    Ban, N.8
  • 39
    • 34547929138 scopus 로고    scopus 로고
    • Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation
    • DOI 10.1083/jcb.200702018
    • Shan SO, Chandrasekar S, Walter P (2007). Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation. J Cell Biol 178, 611-620. (Pubitemid 47267273)
    • (2007) Journal of Cell Biology , vol.178 , Issue.4 , pp. 611-620
    • Shan, S.-O.1    Chandrasekar, S.2    Walter, P.3
  • 40
    • 14544302354 scopus 로고    scopus 로고
    • Co-translational protein targeting by the signal recognition particle
    • Shan SO, Walter P (2005). Co-translational protein targeting by the signal recognition particle. FEBS Lett 579, 921-926.
    • (2005) FEBS Lett , vol.579 , pp. 921-926
    • Shan, S.O.1    Walter, P.2
  • 41
    • 77952331762 scopus 로고    scopus 로고
    • Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting
    • Shen K, Shan SO (2010). Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting. Proc Natl Acad Sci USA 107, 7698-7703.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7698-7703
    • Shen, K.1    Shan, S.O.2
  • 42
    • 79955005771 scopus 로고    scopus 로고
    • Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting
    • Shen K, Zhang X, Shan SO (2011). Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting. RNA 17, 892-902.
    • (2011) RNA , vol.17 , pp. 892-902
    • Shen, K.1    Zhang, X.2    Shan, S.O.3
  • 43
    • 33846456974 scopus 로고    scopus 로고
    • SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting
    • DOI 10.1261/rna.135407
    • Siu FY, Spanggord RJ, Doudna JA (2007). SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting. RNA 13, 240-250. (Pubitemid 46147899)
    • (2007) RNA , vol.13 , Issue.2 , pp. 240-250
    • Siu, F.Y.1    Spanggord, R.J.2    Doudna, J.A.3
  • 44
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 45
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter P, Johnson AE (1994). Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol 10, 87-119. (Pubitemid 24372817)
    • (1994) Annual Review of Cell Biology , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 46
    • 0023740734 scopus 로고
    • Integration of membrane proteins into the endoplasmic reticulum requires GTP
    • Wilson C, Connoly T, Morison T, Gilmore R (1988). Integration of membrane proteins into the endoplasmic reticulum requires GTP. J Cell Biol 107, 67-77.
    • (1988) J Cell Biol , vol.107 , pp. 67-77
    • Wilson, C.1    Connoly, T.2    Morison, T.3    Gilmore, R.4
  • 47
    • 47849117948 scopus 로고    scopus 로고
    • Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: Implications for the catalytic role of SRP RNA
    • Zhang X, Kung S, Shan SO (2008). Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA. J Mol Biol 381, 581-593.
    • (2008) J Mol Biol , vol.381 , pp. 581-593
    • Zhang, X.1    Kung, S.2    Shan, S.O.3
  • 48
    • 77952127782 scopus 로고    scopus 로고
    • Sequential checkpoints govern substrate selection during cotranslational protein targeting
    • Zhang X, Rashid R, Wang K, Shan SO (2010). Sequential checkpoints govern substrate selection during cotranslational protein targeting. Science 328, 757-760.
    • (2010) Science , vol.328 , pp. 757-760
    • Zhang, X.1    Rashid, R.2    Wang, K.3    Shan, S.O.4
  • 49
    • 60549083291 scopus 로고    scopus 로고
    • Multiple conformational switches in a GTPase complex control co-translational protein targeting
    • Zhang X, Schaffitzel C, Ban N, Shan SO (2009). Multiple conformational switches in a GTPase complex control co-translational protein targeting. Proc Natl Acad Sci USA 106, 1754-1759.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1754-1759
    • Zhang, X.1    Schaffitzel, C.2    Ban, N.3    Shan, S.O.4
  • 50
    • 0031310942 scopus 로고    scopus 로고
    • Domain interactions in E. coli SRP: Stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain
    • Zheng N, Gierasch LM (1997). Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain. Mol Cell 1, 79-87. (Pubitemid 127376395)
    • (1997) Molecular Cell , vol.1 , Issue.1 , pp. 79-87
    • Zheng, N.1    Gierasch, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.