메뉴 건너뛰기




Volumn 556, Issue , 2015, Pages 23-49

ACEMBLing a multiprotein transmembrane complex: The functional secyeg-secdf-yajc-yidc holotranslocon protein secretase/insertase

Author keywords

ACEMBL Combinatorial DNA assembly; Holotranslocon; Membrane protein insertion; Membrane proteins; Multiprotein complex; Protein secretion; Protein conducting channel; Recombinant production; Translocation

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN SUBUNIT; RECOMBINANT DNA; SECD PROTEIN, E COLI; SECYEG PROTEIN, E COLI; YIDC PROTEIN, E COLI;

EID: 84940001322     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/bs.mie.2014.12.027     Document Type: Chapter
Times cited : (8)

References (52)
  • 1
    • 0025357506 scopus 로고
    • Secy protein, a membrane-embedded secretion factor of E coli, is cleaved by the ompt protease invitro
    • Y. Akiyama, and K. Ito Secy protein, a membrane-embedded secretion factor of E. coli, is cleaved by the ompt protease invitro Biochemical and Biophysical Research Communications 167 2 1990 711 715
    • (1990) Biochemical and Biophysical Research Communications , vol.167 , Issue.2 , pp. 711-715
    • Akiyama, Y.1    Ito, K.2
  • 2
    • 0028140309 scopus 로고
    • SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation
    • R.A. Arkowitz, and W. Wickner SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation EMBO Journal 13 1994 954 963
    • (1994) EMBO Journal , vol.13 , pp. 954-963
    • Arkowitz, R.A.1    Wickner, W.2
  • 4
    • 0034859711 scopus 로고    scopus 로고
    • YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids
    • K. Beck, G. Eisner, D. Trescher, R.E. Dalbey, J. Brunner, and M. Muller YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids EMBO Reports 2 8 2001 709 714
    • (2001) EMBO Reports , vol.2 , Issue.8 , pp. 709-714
    • Beck, K.1    Eisner, G.2    Trescher, D.3    Dalbey, R.E.4    Brunner, J.5    Muller, M.6
  • 5
    • 0036500974 scopus 로고    scopus 로고
    • The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
    • P. Bessonneau, V. Besson, I. Collinson, and F. Duong The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure EMBO Journal 21 5 2002 995 1003
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 995-1003
    • Bessonneau, P.1    Besson, V.2    Collinson, I.3    Duong, F.4
  • 7
    • 67349278136 scopus 로고    scopus 로고
    • Automated unrestricted multigene recombineering for multiprotein complex production
    • C. Bieniossek, Y. Nie, D. Frey, N. Olieric, C. Schaffitzel, and I. Collinson Automated unrestricted multigene recombineering for multiprotein complex production Nature Methods 6 6 2009 447 450
    • (2009) Nature Methods , vol.6 , Issue.6 , pp. 447-450
    • Bieniossek, C.1    Nie, Y.2    Frey, D.3    Olieric, N.4    Schaffitzel, C.5    Collinson, I.6
  • 8
    • 65249159700 scopus 로고    scopus 로고
    • Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins
    • D. Boy, and H.G. Koch Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins Molecular Biology of the Cell 20 6 2009 1804 1815
    • (2009) Molecular Biology of the Cell , vol.20 , Issue.6 , pp. 1804-1815
    • Boy, D.1    Koch, H.G.2
  • 9
    • 0025087853 scopus 로고
    • The purified E coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation
    • L. Brundage, J.P. Hendrick, E. Schiebel, A.J. Driessen, and W. Wickner The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation Cell 62 4 1990 649 657
    • (1990) Cell , vol.62 , Issue.4 , pp. 649-657
    • Brundage, L.1    Hendrick, J.P.2    Schiebel, E.3    Driessen, A.J.4    Wickner, W.5
  • 10
    • 37549029235 scopus 로고    scopus 로고
    • Mechanism and hydrophobic forces driving membrane protein insertion of subunit II of cytochrome bo 3 oxidase
    • N. Celebi, R.E. Dalbey, and J. Yuan Mechanism and hydrophobic forces driving membrane protein insertion of subunit II of cytochrome bo 3 oxidase Journal of Molecular Biology 375 5 2008 1282 1292
    • (2008) Journal of Molecular Biology , vol.375 , Issue.5 , pp. 1282-1292
    • Celebi, N.1    Dalbey, R.E.2    Yuan, J.3
  • 11
    • 33645077311 scopus 로고    scopus 로고
    • Membrane biogenesis of subunit II of cytochrome bo oxidase: Contrasting requirements for insertion of N-terminal and C-terminal domains
    • N. Celebi, L. Yi, S.J. Facey, A. Kuhn, and R.E. Dalbey Membrane biogenesis of subunit II of cytochrome bo oxidase: Contrasting requirements for insertion of N-terminal and C-terminal domains Journal of Molecular Biology 357 5 2006 1428 1436
    • (2006) Journal of Molecular Biology , vol.357 , Issue.5 , pp. 1428-1436
    • Celebi, N.1    Yi, L.2    Facey, S.J.3    Kuhn, A.4    Dalbey, R.E.5
  • 12
    • 0035873223 scopus 로고    scopus 로고
    • Projection structure and oligomeric properties of a bacterial core protein translocase
    • I. Collinson, C. Breyton, F. Duong, C. Tziatzios, D. Schubert, and E. Or Projection structure and oligomeric properties of a bacterial core protein translocase EMBO Journal 20 10 2001 2462 2471
    • (2001) EMBO Journal , vol.20 , Issue.10 , pp. 2462-2471
    • Collinson, I.1    Breyton, C.2    Duong, F.3    Tziatzios, C.4    Schubert, D.5    Or, E.6
  • 14
    • 0026540532 scopus 로고
    • Precursor protein translocation by the Escherichia-coli translocase is directed by the protonmotive force
    • A.J.M. Driessen Precursor protein translocation by the Escherichia-coli translocase is directed by the protonmotive force EMBO Journal 11 3 1992 847 853
    • (1992) EMBO Journal , vol.11 , Issue.3 , pp. 847-853
    • Driessen, A.J.M.1
  • 15
    • 33744958176 scopus 로고    scopus 로고
    • Subunit a of cytochrome o oxidase requires both YidC and SecYEG for membrane insertion
    • D.J. du Plessis, N. Nouwen, and A.J. Driessen Subunit a of cytochrome o oxidase requires both YidC and SecYEG for membrane insertion Journal of Biological Chemistry 281 18 2006 12248 12252
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12248-12252
    • Du Plessis, D.J.1    Nouwen, N.2    Driessen, A.J.3
  • 16
    • 0030959069 scopus 로고    scopus 로고
    • Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
    • F. Duong, and W. Wickner Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme EMBO Journal 16 10 1997 2756 2768
    • (1997) EMBO Journal , vol.16 , Issue.10 , pp. 2756-2768
    • Duong, F.1    Wickner, W.2
  • 17
    • 0030745847 scopus 로고    scopus 로고
    • The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling
    • F. Duong, and W. Wickner The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling EMBO Journal 16 16 1997 4871 4879
    • (1997) EMBO Journal , vol.16 , Issue.16 , pp. 4871-4879
    • Duong, F.1    Wickner, W.2
  • 18
    • 0029561762 scopus 로고
    • SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
    • A. Economou, J. Pogliano, J. Beckwith, D. Oliver, and W. Wickner SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF Cell 83 7 1995 1171 1181
    • (1995) Cell , vol.83 , Issue.7 , pp. 1171-1181
    • Economou, A.1    Pogliano, J.2    Beckwith, J.3    Oliver, D.4    Wickner, W.5
  • 19
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • D.A. Fancy, and T. Kodadek Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light Proceedings of the National Academy of Sciences of the United States of America 96 11 1999 6020 6024
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.11 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 21
    • 0022532398 scopus 로고
    • Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles
    • B.L. Geller, N.R. Movva, and W. Wickner Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles Proceedings of the National Academy of Sciences of the United States of America 83 12 1986 4219 4222
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.12 , pp. 4219-4222
    • Geller, B.L.1    Movva, N.R.2    Wickner, W.3
  • 23
    • 84884191859 scopus 로고    scopus 로고
    • Tandem recombineering by SLIC cloning and Cre-LoxP fusion to generate multigene expression constructs for protein complex research
    • M. Haffke, C. Viola, Y. Nie, and I. Berger Tandem recombineering by SLIC cloning and Cre-LoxP fusion to generate multigene expression constructs for protein complex research Methods in Molecular Biology 1073 2013 131 140
    • (2013) Methods in Molecular Biology , vol.1073 , pp. 131-140
    • Haffke, M.1    Viola, C.2    Nie, Y.3    Berger, I.4
  • 24
    • 0345444027 scopus 로고    scopus 로고
    • Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation
    • D. Hanein, K. Matlack, B. Jungnickel, K. Plath, K. Kalies, and K. Miller Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation Cell 87 4 1996 721 732
    • (1996) Cell , vol.87 , Issue.4 , pp. 721-732
    • Hanein, D.1    Matlack, K.2    Jungnickel, B.3    Plath, K.4    Kalies, K.5    Miller, K.6
  • 25
    • 0142039007 scopus 로고    scopus 로고
    • Depletion of SecDF-YajC causes a decrease in the level of SecG: Implication for their functional interaction
    • Y. Kato, K. Nishiyama, and H. Tokuda Depletion of SecDF-YajC causes a decrease in the level of SecG: Implication for their functional interaction FEBS Letters 550 1-3 2003 114 118
    • (2003) FEBS Letters , vol.550 , Issue.13 , pp. 114-118
    • Kato, Y.1    Nishiyama, K.2    Tokuda, H.3
  • 26
    • 84901259411 scopus 로고    scopus 로고
    • Structural basis of Sec-independent membrane protein insertion by YidC
    • K. Kumazaki, S. Chiba, M. Takemoto, A. Furukawa, K. Nishiyama, and Y. Sugano Structural basis of Sec-independent membrane protein insertion by YidC Nature 509 7501 2014 516 520
    • (2014) Nature , vol.509 , Issue.7501 , pp. 516-520
    • Kumazaki, K.1    Chiba, S.2    Takemoto, M.3    Furukawa, A.4    Nishiyama, K.5    Sugano, Y.6
  • 27
    • 33847608289 scopus 로고    scopus 로고
    • Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC
    • M.Z. Li, and S.J. Elledge Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC Nature Methods 4 3 2007 251 256
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 251-256
    • Li, M.Z.1    Elledge, S.J.2
  • 30
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • B. Miroux, and J.E. Walker Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels Journal of Molecular Biology 260 3 1996 289 298
    • (1996) Journal of Molecular Biology , vol.260 , Issue.3 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 31
    • 2442585126 scopus 로고    scopus 로고
    • Role of YidC in folding of polytopic membrane proteins
    • S. Nagamori, I.N. Smirnova, and H.R. Kaback Role of YidC in folding of polytopic membrane proteins Journal of Cell Biology 165 1 2004 53 62
    • (2004) Journal of Cell Biology , vol.165 , Issue.1 , pp. 53-62
    • Nagamori, S.1    Smirnova, I.N.2    Kaback, H.R.3
  • 32
    • 0027957715 scopus 로고
    • Genetic and molecular characterization of the Escherichia coli secD operon and its products
    • K.J. Pogliano, and J. Beckwith Genetic and molecular characterization of the Escherichia coli secD operon and its products Journal of Bacteriology 176 3 1994 804 814
    • (1994) Journal of Bacteriology , vol.176 , Issue.3 , pp. 804-814
    • Pogliano, K.J.1    Beckwith, J.2
  • 34
    • 84880071444 scopus 로고    scopus 로고
    • Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER)
    • J.H. Reithinger, J.E. Kim, and H. Kim Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER) The Journal of Biological Chemistry 288 25 2013 18058 18067
    • (2013) The Journal of Biological Chemistry , vol.288 , Issue.25 , pp. 18058-18067
    • Reithinger, J.H.1    Kim, J.E.2    Kim, H.3
  • 35
    • 36048929458 scopus 로고    scopus 로고
    • A large conformational change couples the ATP binding site of SecA to the SecY protein channel
    • A. Robson, A.E. Booth, V.A. Gold, A.R. Clarke, and I. Collinson A large conformational change couples the ATP binding site of SecA to the SecY protein channel Journal of Molecular Biology 374 4 2007 965 976
    • (2007) Journal of Molecular Biology , vol.374 , Issue.4 , pp. 965-976
    • Robson, A.1    Booth, A.E.2    Gold, V.A.3    Clarke, A.R.4    Collinson, I.5
  • 36
    • 84878746549 scopus 로고    scopus 로고
    • YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein
    • I. Sachelaru, N.A. Petriman, R. Kudva, P. Kuhn, T. Welte, and B. Knapp YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein The Journal of Biological Chemistry 288 23 2013 16295 16307
    • (2013) The Journal of Biological Chemistry , vol.288 , Issue.23 , pp. 16295-16307
    • Sachelaru, I.1    Petriman, N.A.2    Kudva, R.3    Kuhn, P.4    Welte, T.5    Knapp, B.6
  • 37
    • 0026073817 scopus 로고
    • Delta mu H + and ATP function at different steps of the catalytic cycle of preprotein translocase
    • E. Schiebel, A.J. Driessen, F.U. Hartl, and W. Wickner Delta mu H + and ATP function at different steps of the catalytic cycle of preprotein translocase Cell 64 5 1991 927 939
    • (1991) Cell , vol.64 , Issue.5 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.2    Hartl, F.U.3    Wickner, W.4
  • 39
    • 0034651753 scopus 로고    scopus 로고
    • YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase
    • P.A. Scotti, M.L. Urbanus, J. Brunner, J.W. de Gier, G. von Heijne, and C. van der Does YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase EMBO Journal 19 4 2000 542 549
    • (2000) EMBO Journal , vol.19 , Issue.4 , pp. 542-549
    • Scotti, P.A.1    Urbanus, M.L.2    Brunner, J.3    De Gier, J.W.4    Von Heijne, G.5    Van Der Does, C.6
  • 41
    • 0025010859 scopus 로고
    • The proton motive force lowers the level of ATP required for the invitro translocation of a secretory protein in Escherichia-coli
    • K. Shiozuka, K. Tani, S. Mizushima, and H. Tokuda The proton motive force lowers the level of ATP required for the invitro translocation of a secretory protein in Escherichia-coli Journal of Biological Chemistry 265 31 1990 18843 18847
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.31 , pp. 18843-18847
    • Shiozuka, K.1    Tani, K.2    Mizushima, S.3    Tokuda, H.4
  • 42
    • 69249146075 scopus 로고    scopus 로고
    • Engineering G protein-coupled receptors to facilitate their structure determination
    • C.G. Tate, and G.F. Schertler Engineering G protein-coupled receptors to facilitate their structure determination Current Opinion in Structural Biology 19 4 2009 386 395
    • (2009) Current Opinion in Structural Biology , vol.19 , Issue.4 , pp. 386-395
    • Tate, C.G.1    Schertler, G.F.2
  • 44
    • 79958281760 scopus 로고    scopus 로고
    • Structure and function of a membrane component SecDF that enhances protein export
    • T. Tsukazaki, H. Mori, Y. Echizen, R. Ishitani, S. Fukai, and T. Tanaka Structure and function of a membrane component SecDF that enhances protein export Nature 474 7350 2011 235 238
    • (2011) Nature , vol.474 , Issue.7350 , pp. 235-238
    • Tsukazaki, T.1    Mori, H.2    Echizen, Y.3    Ishitani, R.4    Fukai, S.5    Tanaka, T.6
  • 46
    • 0034958117 scopus 로고    scopus 로고
    • Sec-dependent membrane protein insertion: Sequential interaction of nascent FtsQ with SecY and YidC
    • M.L. Urbanus, P.A. Scotti, L. Froderberg, A. Saaf, J.W. de Gier, and J. Brunner Sec-dependent membrane protein insertion: Sequential interaction of nascent FtsQ with SecY and YidC EMBO Reports 2 6 2001 524 529
    • (2001) EMBO Reports , vol.2 , Issue.6 , pp. 524-529
    • Urbanus, M.L.1    Scotti, P.A.2    Froderberg, L.3    Saaf, A.4    De Gier, J.W.5    Brunner, J.6
  • 47
    • 42049104126 scopus 로고    scopus 로고
    • Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins
    • E. van Bloois, H.L. Dekker, L. Froderberg, E.N. Houben, M.L. Urbanus, and C.G. de Koster Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins FEBS Letters 582 10 2008 1419 1424
    • (2008) FEBS Letters , vol.582 , Issue.10 , pp. 1419-1424
    • Van Bloois, E.1    Dekker, H.L.2    Froderberg, L.3    Houben, E.N.4    Urbanus, M.L.5    De Koster, C.G.6
  • 49
    • 2142705713 scopus 로고    scopus 로고
    • F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis
    • M. van der Laan, P. Bechtluft, S. Kol, N. Nouwen, and A.J. Driessen F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis Journal of Cell Biology 165 2 2004 213 222
    • (2004) Journal of Cell Biology , vol.165 , Issue.2 , pp. 213-222
    • Van Der Laan, M.1    Bechtluft, P.2    Kol, S.3    Nouwen, N.4    Driessen, A.J.5
  • 52
    • 33750699295 scopus 로고    scopus 로고
    • Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity
    • K. Xie, D. Kiefer, G. Nagler, R.E. Dalbey, and A. Kuhn Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity Biochemistry 45 44 2006 13401 13408
    • (2006) Biochemistry , vol.45 , Issue.44 , pp. 13401-13408
    • Xie, K.1    Kiefer, D.2    Nagler, G.3    Dalbey, R.E.4    Kuhn, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.