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Volumn 8, Issue 2, 2005, Pages 182-187

YidC - An evolutionary conserved device for the assembly of energy-transducing membrane protein complexes

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 15744397061     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2005.02.004     Document Type: Review
Times cited : (53)

References (48)
  • 1
    • 0035856567 scopus 로고    scopus 로고
    • Phylogenetic and structural analyses of the oxa1 family of protein translocases
    • M.R. Yen, K.T. Harley, Y.H. Tseng, and M.H. Saier Jr. Phylogenetic and structural analyses of the oxa1 family of protein translocases FEMS Microbiol Lett 204 2001 223 231
    • (2001) FEMS Microbiol Lett , vol.204 , pp. 223-231
    • Yen, M.R.1    Harley, K.T.2    Tseng, Y.H.3    Saier Jr., M.H.4
  • 2
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/Oxa1/YidC protein family: Membrane-localized chaperones facilitating membrane protein insertion?
    • A. Kuhn, R. Stuart, R. Henry, and R.E. Dalbey The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion? Trends Cell Biol 13 2003 510 516
    • (2003) Trends Cell Biol , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.E.4
  • 3
    • 0030952628 scopus 로고    scopus 로고
    • Membrane translocation of mitochondrially coded Cox2p: Distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p
    • S. He, and T.D. Fox Membrane translocation of mitochondrially coded Cox2p: distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p Mol Biol Cell 8 1997 1449 1460
    • (1997) Mol Biol Cell , vol.8 , pp. 1449-1460
    • He, S.1    Fox, T.D.2
  • 4
    • 0030908894 scopus 로고    scopus 로고
    • Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear-encoded Oxa1p
    • J.M. Herrmann, W. Neupert, and R.A. Stuart Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear-encoded Oxa1p EMBO J 16 1997 2217 2226
    • (1997) EMBO J , vol.16 , pp. 2217-2226
    • Herrmann, J.M.1    Neupert, W.2    Stuart, R.A.3
  • 5
    • 0035868763 scopus 로고    scopus 로고
    • Oxa1 acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA
    • K. Hell, W. Neupert, and R.A. Stuart Oxa1 acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA EMBO J 20 2001 1281 1288
    • (2001) EMBO J , vol.20 , pp. 1281-1288
    • Hell, K.1    Neupert, W.2    Stuart, R.A.3
  • 6
    • 0034695557 scopus 로고    scopus 로고
    • Chloroplast Oxa1p homolog Albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes
    • M. Moore, M.S. Harrison, E.C. Peterson, and R. Henry Chloroplast Oxa1p homolog Albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes J Biol Chem 275 2000 1529 1532
    • (2000) J Biol Chem , vol.275 , pp. 1529-1532
    • Moore, M.1    Harrison, M.S.2    Peterson, E.C.3    Henry, R.4
  • 7
    • 85041115207 scopus 로고    scopus 로고
    • New prospects in studying the bacterial signal recognition particle pathway
    • A.A. Herskovits, E.S. Bochkareva, and E. Bibi New prospects in studying the bacterial signal recognition particle pathway Mol Microbiol 38 2000 927 939
    • (2000) Mol Microbiol , vol.38 , pp. 927-939
    • Herskovits, A.A.1    Bochkareva, E.S.2    Bibi, E.3
  • 8
    • 0026516666 scopus 로고
    • Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion
    • J.I. Lee, A. Kuhn, and R.E. Dalbey Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion J Biol Chem 267 1992 938 943
    • (1992) J Biol Chem , vol.267 , pp. 938-943
    • Lee, J.I.1    Kuhn, A.2    Dalbey, R.E.3
  • 9
    • 0027473683 scopus 로고
    • Sec-dependent and Sec-independent assembly of E. coli inner membrane proteins: The topological rules depend on chain length
    • H. Andersson, and G. von Heijne Sec-dependent and Sec-independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length EMBO J 12 1993 683 691
    • (1993) EMBO J , vol.12 , pp. 683-691
    • Andersson, H.1    Von Heijne, G.2
  • 12
    • 0347087516 scopus 로고    scopus 로고
    • SecYEG proteoliposomes catalyze the Δψ-dependent membrane insertion of FtsQ
    • M. Van der Laan, N. Nouwen, and A.J. Driessen SecYEG proteoliposomes catalyze the Δψ-dependent membrane insertion of FtsQ J Biol Chem 279 2004 1659 1664
    • (2004) J Biol Chem , vol.279 , pp. 1659-1664
    • Van Der Laan, M.1    Nouwen, N.2    Driessen, A.J.3
  • 13
    • 0021233258 scopus 로고
    • Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins
    • P.B. Wolfe, and W. Wickner Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins Cell 36 1984 1067 1072
    • (1984) Cell , vol.36 , pp. 1067-1072
    • Wolfe, P.B.1    Wickner, W.2
  • 14
    • 0028364507 scopus 로고
    • + on the translocation of charged residues explain the 'positive inside' rule
    • + on the translocation of charged residues explain the 'positive inside' rule EMBO J 13 1994 2267 2272
    • (1994) EMBO J , vol.13 , pp. 2267-2272
    • Andersson, H.1    Von Heijne, G.2
  • 15
    • 0028935007 scopus 로고
    • The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: Evidence for an electrophoresis-like membrane transfer mechanism
    • G. Cao, A. Kuhn, and R.E. Dalbey The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism EMBO J 14 1995 866 875
    • (1995) EMBO J , vol.14 , pp. 866-875
    • Cao, G.1    Kuhn, A.2    Dalbey, R.E.3
  • 16
    • 0030953689 scopus 로고    scopus 로고
    • Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane
    • D. Kiefer, X. Hu, R.E. Dalbey, and A. Kuhn Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane EMBO J 16 1997 2197 2204
    • (1997) EMBO J , vol.16 , pp. 2197-2204
    • Kiefer, D.1    Hu, X.2    Dalbey, R.E.3    Kuhn, A.4
  • 17
    • 0033571246 scopus 로고    scopus 로고
    • Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control
    • D. Kiefer, and A. Kuhn Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control EMBO J 18 1999 6299 6306
    • (1999) EMBO J , vol.18 , pp. 6299-6306
    • Kiefer, D.1    Kuhn, A.2
  • 18
    • 0032540320 scopus 로고    scopus 로고
    • The proton motive force, acting on acidic residues, promotes translocation of amino-terminal domains of membrane proteins when the hydrophobicity of the translocation signal is low
    • V.M. Delgado-Partin, and R.E. Dalbey The proton motive force, acting on acidic residues, promotes translocation of amino-terminal domains of membrane proteins when the hydrophobicity of the translocation signal is low J Biol Chem 273 1998 9927 9934
    • (1998) J Biol Chem , vol.273 , pp. 9927-9934
    • Delgado-Partin, V.M.1    Dalbey, R.E.2
  • 19
    • 0034617438 scopus 로고    scopus 로고
    • Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA
    • E.N. Houben, P.A. Scotti, Q.A. Valent, J. Brunner, J.L. de Gier, B. Oudega, and J. Luirink Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA FEBS Lett 476 2000 229 233
    • (2000) FEBS Lett , vol.476 , pp. 229-233
    • Houben, E.N.1    Scotti, P.A.2    Valent, Q.A.3    Brunner, J.4    De Gier, J.L.5    Oudega, B.6    Luirink, J.7
  • 22
    • 0034959718 scopus 로고    scopus 로고
    • Reconstitution of Sec-dependent membrane protein insertion: Nascent FtsQ interacts with YidC in a SecYEG-dependent manner
    • M. Van der Laan, E.N. Houben, N. Nouwen, J. Luirink, and A.J. Driessen Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent manner EMBO Rep 2 2001 519 523
    • (2001) EMBO Rep , vol.2 , pp. 519-523
    • Van Der Laan, M.1    Houben, E.N.2    Nouwen, N.3    Luirink, J.4    Driessen, A.J.5
  • 23
    • 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. Müller YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids EMBO Rep 2 2001 709 714
    • (2001) EMBO Rep , vol.2 , pp. 709-714
    • Beck, K.1    Eisner, G.2    Trescher, D.3    Dalbey, R.E.4    Brunner, J.5    Müller, M.6
  • 25
    • 8844251544 scopus 로고    scopus 로고
    • The two membrane segments of leader peptidase partition one by one into the lipid bilayer via a Sec/YidC interface
    • E.N. Houben, C.M. Ten Hagen-Jongman, J. Brunner, B. Oudega, and J. Luirink The two membrane segments of leader peptidase partition one by one into the lipid bilayer via a Sec/YidC interface EMBO Rep 5 2004 970 975
    • (2004) EMBO Rep , vol.5 , pp. 970-975
    • Houben, E.N.1    Ten Hagen-Jongman, C.M.2    Brunner, J.3    Oudega, B.4    Luirink, J.5
  • 26
    • 0036015653 scopus 로고    scopus 로고
    • SecDFyajC forms a heterotetrameric complex with YidC
    • N. Nouwen, and A.J. Driessen SecDFyajC forms a heterotetrameric complex with YidC Mol Microbiol 44 2002 1397 1405
    • (2002) Mol Microbiol , vol.44 , pp. 1397-1405
    • Nouwen, N.1    Driessen, A.J.2
  • 27
    • 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 J Cell Biol 165 2004 53 62 The role of YidC in the biogenesis of the polytopic membrane protein LacY is analyzed in this paper. YidC is not required for membrane integration of LacY, but needed for its proper folding and stability. This suggests a chaperone-like function of YidC.
    • (2004) J Cell Biol , vol.165 , pp. 53-62
    • Nagamori, S.1    Smirnova, I.N.2    Kaback, H.R.3
  • 28
    • 3843095033 scopus 로고    scopus 로고
    • Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway
    • L. Fröderberg, E.N. Houben, L. Baars, J. Luirink, and J.W. De Gier Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway J Biol Chem 279 2004 31026 31032
    • (2004) J Biol Chem , vol.279 , pp. 31026-31032
    • Fröderberg, L.1    Houben, E.N.2    Baars, L.3    Luirink, J.4    De Gier, J.W.5
  • 30
    • 0035860693 scopus 로고    scopus 로고
    • Function of YidC for the insertion of M13 procoat protein in Escherichia coli: Translocation of mutants that show differences in their membrane potential dependence and Sec requirement
    • J.C. Samuelson, F. Jiang, L. Yi, M. Chen, J.W. De Gier, A. Kuhn, and R.E. Dalbey Function of YidC for the insertion of M13 procoat protein in Escherichia coli: translocation of mutants that show differences in their membrane potential dependence and Sec requirement J Biol Chem 276 2001 34847 34852
    • (2001) J Biol Chem , vol.276 , pp. 34847-34852
    • Samuelson, J.C.1    Jiang, F.2    Yi, L.3    Chen, M.4    De Gier, J.W.5    Kuhn, A.6    Dalbey, R.E.7
  • 31
    • 0038268750 scopus 로고    scopus 로고
    • Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: Different YidC structural requirements for membrane protein insertion
    • M. Chen, K. Xie, N. Nouwen, A.J. Driessen, and R.E. Dalbey Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: different YidC structural requirements for membrane protein insertion J Biol Chem 278 2003 23295 23300
    • (2003) J Biol Chem , vol.278 , pp. 23295-23300
    • Chen, M.1    Xie, K.2    Nouwen, N.3    Driessen, A.J.4    Dalbey, R.E.5
  • 32
    • 0037040894 scopus 로고    scopus 로고
    • Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion
    • M. Chen, J.C. Samuelson, F. Jiang, M. Müller, A. Kuhn, and R.E. Dalbey Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion J Biol Chem 277 2002 7670 7675
    • (2002) J Biol Chem , vol.277 , pp. 7670-7675
    • Chen, M.1    Samuelson, J.C.2    Jiang, F.3    Müller, M.4    Kuhn, A.5    Dalbey, R.E.6
  • 34
    • 0023054119 scopus 로고
    • Both hydrophobic domains of M13 procoat are required to initiate membrane insertion
    • A. Kuhn, G. Kreil, and W. Wickner Both hydrophobic domains of M13 procoat are required to initiate membrane insertion EMBO J 5 1986 3681 3685
    • (1986) EMBO J , vol.5 , pp. 3681-3685
    • Kuhn, A.1    Kreil, G.2    Wickner, W.3
  • 35
    • 0025675488 scopus 로고
    • The function of a leader peptide in translocating charged amino acyl residues across a membrane
    • J. Rohrer, and A. Kuhn The function of a leader peptide in translocating charged amino acyl residues across a membrane Science 250 1990 1418 1421
    • (1990) Science , vol.250 , pp. 1418-1421
    • Rohrer, J.1    Kuhn, A.2
  • 36
    • 0025277448 scopus 로고
    • Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion
    • A. Kuhn, H.Y. Zhu, and R.E. Dalbey Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion EMBO J 9 1990 2385 2388
    • (1990) EMBO J , vol.9 , pp. 2385-2388
    • Kuhn, A.1    Zhu, H.Y.2    Dalbey, R.E.3
  • 42
    • 3142782909 scopus 로고    scopus 로고
    • Efficient assembly of photosystem II in Chlamydomonas reinhardtii requires Alb3.1p, a homolog of Arabidopsis ALBINO3
    • F. Ossenbuhl, V. Gohre, J. Meurer, A. Krieger-Liszkav, J.D. Rochaix, and L.A. Eichacker Efficient assembly of photosystem II in Chlamydomonas reinhardtii requires Alb3.1p, a homolog of Arabidopsis ALBINO3 Plant Cell 16 2004 1790 1800 This study shows that chloroplast Alb3 is not required for integration of the plastid-encoded photosystem II core subunit D1 into the thylakoid membrane of Chlamydomonas reinhardtii, but the assembly of D1 into functional photosystem II complexes is retarded in an Alb3 mutant. Furthermore, levels of nucleus-encoded light-harvesting proteins are vastly reduced while the remaining antenna systems are still connected to photosystem II reaction centers. These data indicate that Alb3 has a dual function and is required for the assembly of both nucleus- and plastid-encoded protein subunits in photosynthetic complexes of C. reinhardtii.
    • (2004) Plant Cell , vol.16 , pp. 1790-1800
    • Ossenbuhl, F.1    Gohre, V.2    Meurer, J.3    Krieger-Liszkav, A.4    Rochaix, J.D.5    Eichacker, L.A.6
  • 43
    • 11244280870 scopus 로고    scopus 로고
    • A homolog of Albino3/Oxa1 is essential for thylakoid biogenesis in the cyanobacterium Synechocystis PCC6803
    • E. Spence, S. Bailey, A. Nenninger, S.G. Moller, and C. Robinson A homolog of Albino3/Oxa1 is essential for thylakoid biogenesis in the cyanobacterium Synechocystis PCC6803 J Biol Chem 279 2004 5572 5580
    • (2004) J Biol Chem , vol.279 , pp. 5572-5580
    • Spence, E.1    Bailey, S.2    Nenninger, A.3    Moller, S.G.4    Robinson, C.5
  • 44
    • 0029925334 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae OXA1 gene is required for the correct assembly of cytochrome c oxidase and oligomycin-sensitive ATP synthase
    • N. Altamura, N. Capitanio, N. Bonnefoy, S. Papa, and G. Dujardin The Saccharomyces cerevisiae OXA1 gene is required for the correct assembly of cytochrome c oxidase and oligomycin-sensitive ATP synthase FEBS Lett 382 1996 111 115
    • (1996) FEBS Lett , vol.382 , pp. 111-115
    • Altamura, N.1    Capitanio, N.2    Bonnefoy, N.3    Papa, S.4    Dujardin, G.5
  • 45
    • 0037115768 scopus 로고    scopus 로고
    • The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana
    • E. Klostermann, I. Droste Gen Helling, J.P. Carde, and D. Schunemann The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana Biochem J 368 2002 777 781
    • (2002) Biochem J , vol.368 , pp. 777-781
    • Klostermann, E.1    Droste Gen Helling, I.2    Carde, J.P.3    Schunemann, D.4
  • 46
    • 0141530036 scopus 로고    scopus 로고
    • Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: Substrate not required
    • M. Moore, R.L. Goforth, H. Mori, and R. Henry Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: substrate not required J Cell Biol 162 2003 1245 1254
    • (2003) J Cell Biol , vol.162 , pp. 1245-1254
    • Moore, M.1    Goforth, R.L.2    Mori, H.3    Henry, R.4
  • 47
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal region of Oxa1
    • L. Jia, M. Dienhart, M. Schramp, M. McCauley, K. Hell, and R.A. Stuart Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1 EMBO J 22 2003 6438 6447 The matrix-localized carboxy terminal domain of Oxa1p binds mitochondrial ribosomes suggesting a co-translational membrane integration mechanism for mitochondrially encoded inner membrane proteins. Truncation of this domain interferes with ribosome binding.
    • (2003) EMBO J , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 48
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • •], this paper also described the binding of mitochondrial ribosomes to the carboxy terminal domain of Oxa1. Furthermore, it demonstrated that the direct ribosome-Oxa1 interaction is crucial for the membrane integration of Cox2, a known Oxa1 substrate.
    • (2003) EMBO J , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.