메뉴 건너뛰기




Volumn 13, Issue 11, 2006, Pages 957-964

Co- and post-translational translocation through the protein-conducting channel: Analogous mechanisms at work?

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; DIMER; POLYPEPTIDE; PROTEIN; PROTEIN SECA; SEC61 PROTEIN; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 33750580851     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1166     Document Type: Review
Times cited : (44)

References (70)
  • 1
    • 0035575592 scopus 로고    scopus 로고
    • Protein trafficking in the exocytic pathway of polarized epithelial cells
    • Nelson, W.J. & Yeaman, C. Protein trafficking in the exocytic pathway of polarized epithelial cells. Trends Cell Biol. 11, 483-486 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 483-486
    • Nelson, W.J.1    Yeaman, C.2
  • 2
    • 1642570286 scopus 로고    scopus 로고
    • Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol
    • Mitra, K., Ubarretxena-Belandia, I., Taguchi, T., Warren, G. & Engelman, D.M. Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol. Proc. Natl. Acad. Sci. USA 101, 4083-4088 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4083-4088
    • Mitra, K.1    Ubarretxena-Belandia, I.2    Taguchi, T.3    Warren, G.4    Engelman, D.M.5
  • 3
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S.M. & Blobel, G. A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380 (1991).
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 4
    • 0025885002 scopus 로고
    • The enzymology of protein translocation across the Escherichia coli plasma membrane
    • Wickner, W., Driessen, A.J.M. & Hartl, F.U. The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu. Rev. Biochem. 60, 101-124 (1991).
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 101-124
    • Wickner, W.1    Driessen, A.J.M.2    Hartl, F.U.3
  • 6
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou, A. & Wickner, W. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78, 835-843 (1994).
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 7
    • 0028997459 scopus 로고
    • Post-translational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
    • Panzner, S., Dreier, L., Hartmann, E., Kostka, S. & Rapoport, T.A. Post-translational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81, 561-570 (1995).
    • (1995) Cell , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 8
    • 0347192985 scopus 로고    scopus 로고
    • X-ray structure of a protein-conducting channel
    • van den Berg, B. et al. X-ray structure of a protein-conducting channel. Nature 427, 36-44 (2004).
    • (2004) Nature , vol.427 , pp. 36-44
    • Van Den Berg, B.1
  • 9
    • 27844444793 scopus 로고    scopus 로고
    • Structure of the E. coli protein-conducting channel bound to a translating ribosome
    • Mitra, K. et al. Structure of the E. coli protein-conducting channel bound to a translating ribosome. Nature 438, 318-324 (2005).
    • (2005) Nature , vol.438 , pp. 318-324
    • Mitra, K.1
  • 10
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G. & Dobberstein, B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 835-851 (1975).
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 11
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • von Heijne, G. Signal sequences. The limits of variation. J. Mol. Biol. 184, 99-105 (1985).
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 13
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: Interactions of SRP and trigger factor with nascent polypeptides
    • Valent, Q.A. et al. Early events in preprotein recognition in E. coli: interactions of SRP and trigger factor with nascent polypeptides. EMBO J. 14, 5494-5505 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5494-5505
    • Valent, Q.A.1
  • 14
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum
    • Ng, D.T.W., Brown, J.D. & Walter, P. Signal sequences specify the targeting route to the endoplasmic reticulum. J. Cell Biol. 134, 269-278 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 269-278
    • Ng, D.T.W.1    Brown, J.D.2    Walter, P.3
  • 15
    • 0024450987 scopus 로고
    • Helix formation and stability in a signal sequence
    • Bruch, M.D., McKnight, C.J. & Gierasch, L.M. Helix formation and stability in a signal sequence. Biochemistry 28, 8554-8561 (1989).
    • (1989) Biochemistry , vol.28 , pp. 8554-8561
    • Bruch, M.D.1    McKnight, C.J.2    Gierasch, L.M.3
  • 16
    • 0034631835 scopus 로고    scopus 로고
    • Role of the cytoplasmic segments of Sec61α in the ribosome-binding and translocation-promoting activities of the Sec61 complex
    • Raden, D., Song, W. & Gilmore, R. Role of the cytoplasmic segments of Sec61α in the ribosome-binding and translocation-promoting activities of the Sec61 complex. J. Cell Biol. 150, 53-64 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 53-64
    • Raden, D.1    Song, W.2    Gilmore, R.3
  • 17
    • 12144272096 scopus 로고    scopus 로고
    • Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation
    • Cheng, Z., Jiang, Y., Mandon, E.C. & Gilmore, R. Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation. J. Cell Biol. 168, 67-77 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 67-77
    • Cheng, Z.1    Jiang, Y.2    Mandon, E.C.3    Gilmore, R.4
  • 18
    • 1842561598 scopus 로고    scopus 로고
    • The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells
    • Snapp, E.L., Reinhart, G.A., Bogert, B.A., Lippincott-Schwartz, J. & Hegde, R.S. The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells. J. Cell Biol. 164, 997-1007 (2004).
    • (2004) J. Cell Biol. , vol.164 , pp. 997-1007
    • Snapp, E.L.1    Reinhart, G.A.2    Bogert, B.A.3    Lippincott-Schwartz, J.4    Hegde, R.S.5
  • 19
    • 0036500974 scopus 로고    scopus 로고
    • The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
    • Bessonneau, P., Besson, V., Collinson, I. & Duong, F. The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure. EMBO J. 21, 995-1003 (2002).
    • (2002) EMBO J. , vol.21 , pp. 995-1003
    • Bessonneau, P.1    Besson, V.2    Collinson, I.3    Duong, F.4
  • 20
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann, R. et al. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell 107, 361-372 (2001).
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1
  • 21
    • 0036927080 scopus 로고    scopus 로고
    • Structure of the mammalian ribosome-channel complex at 17 Å resolution
    • Morgan, D.G., Menetret, J.-F., Neuhof, A., Rapoport, T.A. & Akey, C.W. Structure of the mammalian ribosome-channel complex at 17 Å resolution. J. Mol. Biol. 324, 871-886 (2002).
    • (2002) J. Mol. Biol. , vol.324 , pp. 871-886
    • Morgan, D.G.1    Menetret, J.-F.2    Neuhof, A.3    Rapoport, T.A.4    Akey, C.W.5
  • 22
    • 27644518797 scopus 로고    scopus 로고
    • The oligomeric distribution of SecYEG is altered by SecA and translocation ligands
    • Scheuring, J. et al. The oligomeric distribution of SecYEG is altered by SecA and translocation ligands. J. Mol. Biol. 354, 258-271 (2005).
    • (2005) J. Mol. Biol. , vol.354 , pp. 258-271
    • Scheuring, J.1
  • 23
    • 0016752682 scopus 로고
    • Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components
    • Blobel, G. & Dobberstein, B. Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67, 852-862 (1975).
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 24
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M.W., Brunner, J. & Dobberstein, B. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81, 207-214 (1995).
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 25
    • 0025005885 scopus 로고
    • Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization
    • Tani, K., Tokuda, H. & Mizushima, S. Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization. J. Biol. Chem. 265, 17341-17347 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 17341-17347
    • Tani, K.1    Tokuda, H.2    Mizushima, S.3
  • 26
    • 33646931831 scopus 로고    scopus 로고
    • A model for co-translational translocation: Ribosome-regulated nascent polypeptide translocation at the protein-conducting channel
    • Mitra, K. & Frank, J. A model for co-translational translocation: ribosome-regulated nascent polypeptide translocation at the protein-conducting channel. FEBS Lett. 580, 3353-3360 (2006).
    • (2006) FEBS Lett. , vol.580 , pp. 3353-3360
    • Mitra, K.1    Frank, J.2
  • 27
    • 0040038098 scopus 로고
    • Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli
    • Simon, S.M., Blobel, G. & Zimmerberg, J. Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 86, 6176-6180 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6176-6180
    • Simon, S.M.1    Blobel, G.2    Zimmerberg, J.3
  • 28
    • 0034697967 scopus 로고    scopus 로고
    • The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich, S.U., Mothes, W., Brunner, J. & Rapoport, T.A. The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell 102, 233-244 (2000).
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.U.1    Mothes, W.2    Brunner, J.3    Rapoport, T.A.4
  • 29
    • 0024400708 scopus 로고
    • Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
    • Romisch, K. et al. 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).
    • (1989) Nature , vol.340 , pp. 478-482
    • Romisch, K.1
  • 30
    • 0009499348 scopus 로고
    • Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
    • Walter, P. & Blobel, G. Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 77, 7112-7116 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7112-7116
    • Walter, P.1    Blobel, G.2
  • 31
    • 0034602866 scopus 로고    scopus 로고
    • Role of Sec61α in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel
    • Song, W., Raden, D., Mandon, E.C. & Gilmore, R. Role of Sec61α in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel. Cell 100, 333-343 (2000).
    • (2000) Cell , vol.100 , pp. 333-343
    • Song, W.1    Raden, D.2    Mandon, E.C.3    Gilmore, R.4
  • 33
    • 0030814881 scopus 로고    scopus 로고
    • A GTP-binding protein of Mycoplasma hominis: A small sized homolog to the signal recognition particle receptor FtsY
    • Ladefoged, S.A. & Christiansen, G. A GTP-binding protein of Mycoplasma hominis: a small sized homolog to the signal recognition particle receptor FtsY. Gene 201, 37-44 (1997).
    • (1997) Gene , vol.201 , pp. 37-44
    • Ladefoged, S.A.1    Christiansen, G.2
  • 34
    • 0019217428 scopus 로고
    • Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum
    • Meyer, D.I. & Dobberstein, B. Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum. J. Cell Biol. 87, 503-508 (1980).
    • (1980) J. Cell Biol. , vol.87 , pp. 503-508
    • Meyer, D.I.1    Dobberstein, B.2
  • 35
    • 0029963973 scopus 로고    scopus 로고
    • Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
    • Bacher, G., Lutcke, H., Jungnickel, B., Rapoport, T.A. & Dobberstein, B. Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Nature 381, 248-251 (1996).
    • (1996) Nature , vol.381 , pp. 248-251
    • Bacher, G.1    Lutcke, H.2    Jungnickel, B.3    Rapoport, T.A.4    Dobberstein, B.5
  • 36
    • 0038268408 scopus 로고    scopus 로고
    • The β-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the β-subunit of the signal recognition particle receptor
    • Helmers, J., Schmidt, D., Glavy, J.S., Blobel, G. & Schwartz, T. The β-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the β-subunit of the signal recognition particle receptor. J. Biol. Chem. 278, 23686-23690 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 23686-23690
    • Helmers, J.1    Schmidt, D.2    Glavy, J.S.3    Blobel, G.4    Schwartz, T.5
  • 37
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic, M. et al. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427, 808-814 (2004).
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1
  • 38
    • 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
  • 39
    • 20044388542 scopus 로고    scopus 로고
    • FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon
    • Angelini, S., Deitermann, S. & Koch, H.G. FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon. EMBO Rep. 6, 476-481 (2005).
    • (2005) EMBO Rep. , vol.6 , pp. 476-481
    • Angelini, S.1    Deitermann, S.2    Koch, H.G.3
  • 40
    • 0034282447 scopus 로고    scopus 로고
    • Nucleotide-dependent bindingj of the GTPase domain of the signal recognition particle receptor β-subunit to the α-subunit
    • Legate, K.R., Falcone, D. & Andrews, D.W. Nucleotide-dependent bindingj of the GTPase domain of the signal recognition particle receptor β-subunit to the α-subunit. J. Biol. Chem. 275, 27439-27446 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27439-27446
    • Legate, K.R.1    Falcone, D.2    Andrews, D.W.3
  • 41
    • 0037459447 scopus 로고    scopus 로고
    • Structural basis for the function of the β subunit of the eukaryotic signal recognition particle receptor
    • Schwartz, T. & Blobel, G. Structural basis for the function of the β subunit of the eukaryotic signal recognition particle receptor. Cell 112, 793-803 (2003).
    • (2003) Cell , vol.112 , pp. 793-803
    • Schwartz, T.1    Blobel, G.2
  • 42
    • 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
  • 44
    • 0029097359 scopus 로고
    • Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
    • Powers, T. & Walter, P. Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 269, 1422-1424 (1995).
    • (1995) Science , vol.269 , pp. 1422-1424
    • Powers, T.1    Walter, P.2
  • 45
    • 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. & Dobberstein, B. Distinct modes of signal recognition particle interaction with the ribosome. Science 297, 1345-1348 (2002).
    • (2002) Science , vol.297 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 46
    • 0033598154 scopus 로고    scopus 로고
    • The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor
    • Bacher, G., Pool, M. & Dobberstein, B. The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor. J. Cell Biol. 146, 723-730 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 723-730
    • Bacher, G.1    Pool, M.2    Dobberstein, B.3
  • 47
    • 0035341399 scopus 로고    scopus 로고
    • SRb coordinates signal sequence release from SRP with ribosome binding to the translocon
    • Fulga, T.A., Sinning, I., Dobberstein, B. & Pool, M.R. SRb coordinates signal sequence release from SRP with ribosome binding to the translocon. EMBO J. 20, 2338-2347 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2338-2347
    • Fulga, T.A.1    Sinning, I.2    Dobberstein, B.3    Pool, M.R.4
  • 48
    • 0023737896 scopus 로고
    • Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum
    • Shaw, A.S., Rottier, P.J.M. & Rose, J.K. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 85, 7592-7596 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7592-7596
    • Shaw, A.S.1    Rottier, P.J.M.2    Rose, J.K.3
  • 49
    • 33646524478 scopus 로고    scopus 로고
    • Elongation arrest by SecM via a cascade of ribosomal RNA rearrangements
    • Mitra, K. et al. Elongation arrest by SecM via a cascade of ribosomal RNA rearrangements. Mol. Cell 22, 533-543 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 533-543
    • Mitra, K.1
  • 50
    • 0041528498 scopus 로고    scopus 로고
    • Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen
    • Rutkowski, D.T., Ott, C.M., Polansky, J.R. & Lingappa, V.R. Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen. J. Biol. Chem. 278, 30365-30372 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 30365-30372
    • Rutkowski, D.T.1    Ott, C.M.2    Polansky, J.R.3    Lingappa, V.R.4
  • 51
    • 0037184082 scopus 로고    scopus 로고
    • YidC and SecY mediate membrane insertion of a type I transmembrane domain
    • Houben, E.N. et al. YidC and SecY mediate membrane insertion of a type I transmembrane domain. J. Biol. Chem. 277, 35880-35886 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 35880-35886
    • Houben, E.N.1
  • 52
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • Hunt, J.F. et al. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 297, 2018-2026 (2002).
    • (2002) Science , vol.297 , pp. 2018-2026
    • Hunt, J.F.1
  • 53
    • 0345184333 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase
    • Sharma, V. et al. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase. Proc. Natl. Acad. Sci. USA 100, 2243-2248 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2243-2248
    • Sharma, V.1
  • 54
    • 1842690648 scopus 로고    scopus 로고
    • Binding of SecA to the SecYEG complex accelerates the nucleotide exchange kinetics on SecA
    • Natale, P., Swaving, J., de Keyzer, J., van der Does, C. & Driessen, A.J.M. Binding of SecA to the SecYEG complex accelerates the nucleotide exchange kinetics on SecA. J. Biol. Chem. 279, 13769-13777 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 13769-13777
    • Natale, P.1    Swaving, J.2    De Keyzer, J.3    Van Der Does, C.4    Driessen, A.J.M.5
  • 55
    • 0024461425 scopus 로고
    • SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli
    • Lill, R. et al. SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli. EMBO J. 8, 961-966 (1989).
    • (1989) EMBO J. , vol.8 , pp. 961-966
    • Lill, R.1
  • 56
    • 0026073817 scopus 로고
    • ΔμH+ and ATP function at different steps of the catalytic cyle of preprotein translocase
    • Schiebel, E., Driessen, A.J.M., Hartl, F.U. & Wickner, W. ΔμH+ and ATP function at different steps of the catalytic cyle of preprotein translocase. Cell 64, 927-939 (1991).
    • (1991) Cell , vol.64 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.M.2    Hartl, F.U.3    Wickner, W.4
  • 57
    • 0031435335 scopus 로고    scopus 로고
    • The catalytic cycle of the Escherichia coli SecA ATPase comprises two distinct preprotein translocation events
    • van Der Wolk, J.P., de Wit, J.G. & Driessen, A.J.M. The catalytic cycle of the Escherichia coli SecA ATPase comprises two distinct preprotein translocation events. EMBO J. 16, 7297-7304 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7297-7304
    • Van Der Wolk, J.P.1    De Wit, J.G.2    Driessen, A.J.M.3
  • 58
    • 0033675260 scopus 로고    scopus 로고
    • Crystal structure of the bactieral protein export chaperone SecB
    • Xu, Z., Knafels, J.D. & Yoshino, K. Crystal structure of the bactieral protein export chaperone SecB. Nat. Struct. Biol. 7, 1172-1177 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1172-1177
    • Xu, Z.1    Knafels, J.D.2    Yoshino, K.3
  • 59
    • 0041154140 scopus 로고    scopus 로고
    • Substrate specificity of the SecB chaperone
    • Knoblauch, N.T. et al. Substrate specificity of the SecB chaperone. J. Biol. Chem. 274, 34219-34225 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 34219-34225
    • Knoblauch, N.T.1
  • 60
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
    • Fekkes, P., van der Does, C. & Driessen, A.J.M. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. EMBO J. 16, 6105-6113 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6105-6113
    • Fekkes, P.1    Van Der Does, C.2    Driessen, A.J.M.3
  • 61
    • 0242407175 scopus 로고    scopus 로고
    • Structural determinants of SecB recognition by SecA in bacterial protein translocation
    • Zhou, J. & Xu, Z. Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nat. Struct. Biol. 10, 942-947 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 942-947
    • Zhou, J.1    Xu, Z.2
  • 62
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl, F.U., Lecker, S., Schiebel, E., Hendrick, J.P. & Wickner, W. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63, 269-279 (1990).
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 63
    • 0037134449 scopus 로고    scopus 로고
    • Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain
    • Baud, C. et al. Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain. J. Biol. Chem. 277, 13724-13731 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 13724-13731
    • Baud, C.1
  • 64
    • 2542450771 scopus 로고    scopus 로고
    • Global coordination of protein translocation by the SecA IRA1 switch
    • Vrontou, E., Karamanou, S., Baud, C., Sianidis, G. & Economou, A. Global coordination of protein translocation by the SecA IRA1 switch. J. Biol. Chem. 279, 22490-22497 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 22490-22497
    • Vrontou, E.1    Karamanou, S.2    Baud, C.3    Sianidis, G.4    Economou, A.5
  • 65
    • 33746905934 scopus 로고    scopus 로고
    • Identification of two interaction sites in SecY that are important for the functional interaction with SecA
    • van der Sluis, E.O. et al. Identification of two interaction sites in SecY that are important for the functional interaction with SecA. J. Mol. Biol. 361, 839-849 (2006).
    • (2006) J. Mol. Biol. , vol.361 , pp. 839-849
    • Van Der Sluis, E.O.1
  • 66
    • 2942733422 scopus 로고    scopus 로고
    • The baterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules
    • Tziatzios, C. et al. The baterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules. J. Mol. Biol. 340, 513-524 (2004).
    • (2004) J. Mol. Biol. , vol.340 , pp. 513-524
    • Tziatzios, C.1
  • 67
    • 27444439568 scopus 로고    scopus 로고
    • Covalently dimerized SecA is functional in protein translocation
    • de Keyzer, J. et al. Covalently dimerized SecA is functional in protein translocation. J. Biol. Chem. 280, 35255-35260 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 35255-35260
    • De Keyzer, J.1
  • 69
    • 17844377305 scopus 로고    scopus 로고
    • Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy
    • Natale, P., den Blaauwen, T., van der Does, C. & Driessen, A.J.M. Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy. Biochemistry 44, 6424-6432 (2005).
    • (2005) Biochemistry , vol.44 , pp. 6424-6432
    • Natale, P.1    Den Blaauwen, T.2    Van Der Does, C.3    Driessen, A.J.M.4
  • 70
    • 0037423278 scopus 로고    scopus 로고
    • Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA
    • Benach, J. et al. Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. J. Biol. Chem. 278, 3628-3638 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 3628-3638
    • Benach, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.