The protein-conducting channel SecYEG

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1694, Issue 1-3 SPEC.ISS., 2004, Pages 81-95

  Veenendaal, Andreas K J ^a   Van Der Does, Chris ^a   Driessen, Arnold J M ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

Protein translocation; Protein conducting channel; Secretion; SecYEG; Translocase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CARRIER PROTEIN; MEMBRANE PROTEIN; PROTEIN; PROTEIN SUBUNIT; SECE PROTEIN; SECG PROTEIN; SECY PROTEIN; SECYEG PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; DYNAMICS; GENE EXPRESSION; GENE TRANSLOCATION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; RIBOSOME; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN SUBUNITS;

ARCHAEA; EUKARYOTA;

EID: 8844230242     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.02.009     Document Type: Review

References (177)

1. Driessen A.J.M., Manting E.H., van der Does C. The structural basis of protein targeting and translocation in bacteria. Nat. Struct. Biol. 8:2001;492-498
2. Economou A. Bacterial protein translocase: a unique molecular machine with an army of substrates. FEBS Lett. 476:2000;18-21
3. Oliver D.B., Beckwith J. E. coli mutant pleiotropically defective in the export of secreted proteins. Cell. 25:1981;765-772
4. Ito K., Wittekind M., Nomura M., Shiba K., Yura T., Miura A., Nashimoto H. A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins. Cell. 32:1983;789-797
5. Riggs P.D., Derman A.I., Beckwith J. A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene. Genetics. 118:1988;571-579
6. Nishiyama K., Hanada M., Tokuda H. Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature. EMBO J. 13:1994;3272-3277
7. Prinz A., Behrens C., Rapoport T.A., Hartmann E., Kalies K.U. Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA. EMBO J. 19:2000;1900-1906
8. Zito C.R., Oliver D. Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction. J. Biol. Chem. 278:2003;40640-40646
9. Gardel C., Benson S., Hunt J., Michaelis S., Beckwith J. secD, a new gene involved in protein export in Escherichia coli. J. Bacteriol. 169:1987;1286-1290
10. Gardel C., Johnson K., Jacq A., Beckwith J. The secD locus of E. coli codes for two membrane proteins required for protein export. EMBO J. 9:1990;3209-3216
11. Pogliano K.J., Beckwith J. Genetic and molecular characterization of the Escherichia coli secD operon and its products. J. Bacteriol. 176:1994;804-814
12. Duong F., Wickner W. Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. EMBO J. 16:1997;2756-2768
13. Gorlich D., Rapoport T.A. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell. 75:1993;615-630
14. Nakai M., Tanaka A., Omata T., Endo T. Cloning and characterization of the secY gene from the cyanobacterium Synechococcus PCC7942. Biochim. Biophys. Acta. 1171:1992;113-116
15. Scaramuzzi C.D., Stokes H.W., Hiller R.G. Characterisation of a chloroplast-encoded secY homologue and atpH from a chromophytic alga. Evidence for a novel chloroplast genome organisation. FEBS Lett. 304:1992;119-123
16. Laidler V., Chaddock A.M., Knott T.G., Walker D., Robinson C. A SecY homolog in Arabidopsis thaliana. Sequence of a full-length cDNA clone and import of the precursor protein into chloroplasts. J. Biol. Chem. 270:1995;17664-17667
17. Schuenemann D., Amin P., Hartmann E., Hoffman N.E. Chloroplast SecY Is Complexed to SecE and Involved in the Translocation of the 33-kDa but Not the 23-kDa Subunit of the Oxygen-evolving Complex. J. Biol. Chem. 274:1999;12177-12182
18. Nakai M., Nohara T., Sugita D., Endo T. Identification and characterization of the sec-A protein homologue in the cyanobacterium Synechococcus PCC7942. Biochem. Biophys. Res. Commun. 200:1994;844-851
19. Nakai M., Goto A., Nohara T., Sugita D., Endo T. Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J. Biol. Chem. 269:1994;31338-31341
20. Auer J., Spicker G., Bock A. Presence of a gene in the archaebacterium Methanococcus vannielii homologous to secY of eubacteria. Biochimie. 73:1991;683-688
21. Arndt E. The genes for ribosomal protein L15 and the protein equivalent to secY in the archaebacterium Haloarcula (Halobacterium) marismortui. Biochim. Biophys. Acta. 1130:1992;113-116
22. Kath T., Schafer G. A secY homologous gene in the crenarchaeon Sulfolobus acidocaldarius. Biochim. Biophys. Acta. 1264:1995;155-158
23. Kinch L.N., Saier M.H. Jr., Grishin N.V. Sec61beta - a component of the archaeal protein secretory system. Trends Biochem. Sci. 27:2002;170-171
24. Emr S.D., Hanley-Way S., Silhavy T.J. Suppressor mutations that restore export of a protein with a defective signal sequence. Cell. 23:1981;79-88
25. Bankaitis V.A., Bassford P.J. Jr. Proper interaction between at least two components is required for efficient export of proteins to the Escherichia coli cell envelope. J. Bacteriol. 161:1985;169-178
26. Stader J., Gansheroff L.J., Silhavy T.J. New suppressors of signal-sequence mutations, prlG, are linked tightly to the secE gene of Escherichia coli. Genes Dev. 3:1989;1045-1052
27. Cabelli R.J., Chen L., Tai P.C., Oliver D.B. SecA protein is required for secretory protein translocation into E. coli membrane vesicles. Cell. 55:1988;683-692
28. Brundage L., Hendrick J.P., Schiebel E., Driessen A.J.M., Wickner W. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell. 62:1990;649-657
29. Akimaru J., Matsuyama S., Tokuda H., Mizushima S. Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 88:1991;6545-6549
30. Douville K., Leonard M., Brundage L., Nishiyama K., Tokuda H., Mizushima S., Wickner W. Band 1 subunit of Escherichia coli preprotein translocase and integral membrane export factor P12 are the same protein. J. Biol. Chem. 269:1994;18705-18707
31. Nishiyama K., Mizushima S., Tokuda H. A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli. EMBO J. 12:1993;3409-3415
32. Bonnefoy N., Chalvet F., Hamel P., Slonimski P.P., Dujardin G. OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis. J. Mol. Biol. 239:1994;201-212
33. Hell K., Herrmann J., Pratje E., Neupert W., Stuart R.A. Oxa1p mediates the export of the N- and C-termini of pCoxII from the mitochondrial matrix to the intermembrane space. FEBS Lett. 418:1997;367-370
34. Hell K., Neupert W., Stuart R.A. Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA. EMBO J. 20:2001;1281-1288
35. Samuelson J.C., Chen M., Jiang F., Moller I., Wiedmann M., Kuhn A., Phillips G.J., Dalbey R.E. YidC mediates membrane protein insertion in bacteria. Nature. 406:2000;637-641
36. Scotti P.A., Urbanus M.L., Brunner J., de Gier J.W., von Heijne G., van der Does C., Driessen A.J.M., Oudega B., Luirink J. YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. EMBO J. 19:2000;542-549
37. Nouwen N., Driessen A.J.M. SecDFyajC forms a heterotetrameric complex with YidC. Mol. Microbiol. 44:2002;1397-1405
38. Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Res. 11:1983;2599-2616
39. Akiyama Y., Ito K. Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli. EMBO J. 6:1987;3465-3470
40. Hartmann E., Sommer T., Prehn S., Gorlich D., Jentsch S., Rapoport T.A. Evolutionary conservation of components of the protein translocation complex. Nature. 367:1994;654-657
41. Pohlschroder M., Prinz W.A., Hartmann E., Beckwith J. Protein translocation in the three domains of life: variations on a theme. Cell. 91:1997;563-566
42. Eichler J. Archaeal protein translocation crossing membranes in the third domain of life. Eur. J. Biochem. 267:2000;3402-3412
43. Shimoike T., Akiyama Y., Baba T., Taura T., Ito K. SecY variants that interfere with Escherichia coli protein export in the presence of normal SecY. Mol. Microbiol. 6:1992;1205-1210
44. Mori H., Ito K. An essential amino acid residue in the protein translocation channel revealed by targeted random mutagenesis of SecY. Proc. Natl. Acad. Sci. U. S. A. 98:2001;5128-5133
45. Emr S.D., Bassford P.J. Jr. Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. J. Biol. Chem. 257:1982;5852-5860
46. Stader J., Benson S.A., Silhavy T.J. Kinetic analysis of lamB mutants suggests the signal sequence plays multiple roles in protein export. J. Biol. Chem. 261:1986;15075-15080
47. Puziss J.W., Strobel S.M., Bassford P.J. Jr. Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations. J. Bacteriol. 174:1992;92-101
48. Osborne R.S., Silhavy T.J. PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains. EMBO J. 12:1993;3391-3398
49. Francetic O., Hanson M.P., Kumamoto C.A. prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli. J. Bacteriol. 175:1993;4036-4044
50. Olsen M.K., Rosey E.L., Tomich C.S. Isolation and analysis of novel mutants of Escherichia coli prlA (secY). J. Bacteriol. 175:1993;7092-7096
51. Derman A.I., Puziss J.W., Bassford P.J. Jr., Beckwith J. A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J. 12:1993;879-888
52. Flower A.M., Doebele R.C., Silhavy T.J. PrlA and PrlG suppressors reduce the requirement for signal sequence recognition. J. Bacteriol. 176:1994;5607-5614
53. Prinz W.A., Spiess C., Ehrmann M., Schierle C., Beckwith J. Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase. EMBO J. 15:1996;5209-5217
54. van der Wolk J.P., Fekkes P., Boorsma A., Huie J.L., Silhavy T.J., Driessen A.J.M. PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation. EMBO J. 17:1998;3631-3639
55. Iino T., Sako T. Inhibition and resumption of processing of the staphylokinase in some Escherichia coli prlA suppressor mutants. J. Biol. Chem. 263:1988;19077-19082
56. Sako T., Iino T. Distinct mutation sites in prlA suppressor mutant strains of Escherichia coli respond either to suppression of signal peptide mutations or to blockage of staphylokinase processing. J. Bacteriol. 170:1988;5389-5391
57. Schatz P.J., Riggs P.D., Jacq A., Fath M.J., Beckwith J. The secE gene encodes an integral membrane protein required for protein export in Escherichia coli. Genes Dev. 3:1989;1035-1044
58. Murphy C.K., Beckwith J. Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region. Proc. Natl. Acad. Sci. U. S. A. 91:1994;2557-2561
59. Schatz P.J., Bieker K.L., Ottemann K.M., Silhavy T.J., Beckwith J. One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery. EMBO J. 10:1991;1749-1757
60. Nishiyama K., Mizushima S., Tokuda H. The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli. J. Biol. Chem. 267:1992;7170-7176
61. Jeong S.M., Yoshikawa H., Takahashi H. Isolation and characterization of the secE homologue gene of Bacillus subtilis. Mol. Microbiol. 10:1993;133-142
62. Froderberg L., Rohl T., van Wijk K.J., de Gier J.W. Complementation of bacterial SecE by a chloroplastic homologue. FEBS Lett. 498:2001;52-56
63. Matsuo E., Mori H., Ito K. Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states. Mol. Genet. Genomics. 268:2003;808-815
64. Pohlschroder M., Murphy C., Beckwith J. In vivo analyses of interactions between SecE and SecY, core components of the Escherichia coli protein translocation machinery. J. Biol. Chem. 271:1996;19908-19914
65. Kontinen V.P., Yamanaka M., Nishiyama K., Tokuda H. Roles of the conserved cytoplasmic region and non-conserved carboxy-terminal region of SecE in Escherichia coli protein translocase. J. Biochem. (Tokyo). 119:1996;1124-1130
66. Nishiyama K., Suzuki T., Tokuda H. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell. 85:1996;71-81
67. Bost S., Belin D. A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery. EMBO J. 14:1995;4412-4421
68. Flower A.M., Hines L.L., Pfennig P.L. SecG is an auxiliary component of the protein export apparatus of Escherichia coli. Mol. Gen. Genet. 263:2000;131-136
69. Hanada M., Nishiyama K., Tokuda H. SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature. FEBS Lett. 381:1996;25-28
70. Nagamori S., Nishiyama K., Tokuda H. Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA. J. Biochem. (Tokyo). 132:2002;629-634
71. Nagamori S., Nishiyama K., Tokuda H. Two SecG molecules present in a single protein translocation machinery are functional even after cross-linking. J. Biochem. 128:2000;129-137
72. Suzuki H., Nishiyama K., Tokuda H. Coupled structure changes of SecA and SecG revealed by the synthetic lethality of the secAcsR11 and delta secG::kan double mutant. Mol. Microbiol. 29:1998;331-341
73. Matsumoto G., Mori H., Ito K. Roles of SecG in ATP- and SecA-dependent protein translocation. Proc. Natl. Acad. Sci. U. S. A. 95:1998;13567-13572
74. Kontinen V.P., Tokuda H. Overexpression of phosphatidylglycerophosphate synthase restores protein translocation in a secG deletion mutant of Escherichia coli at low temperature. FEBS Lett. 364:1995;157-160
75. Shimizu H., Nishiyama K., Tokuda H. Expression of gpsA encoding biosynthetic sn-glycerol 3-phosphate dehydrogenase suppresses both the LB-phenotype of a secB null mutant and the cold-sensitive phenotype of a secG null mutant. Mol. Microbiol. 26:1997;1013-1021
76. Bost S., Belin D. prl mutations in the Escherichia coli secG gene. J. Biol. Chem. 272:1997;4087-4093
77. Bost S., Silva F., Rudaz C., Belin D. Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery. Mol. Microbiol. 38:2000;575-587
78. Cabelli R.J., Dolan K.M., Qian L.P., Oliver D.B. Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli. J. Biol. Chem. 266:1991;24420-24427
79. Akita M., Shinaki A., Matsuyama S., Mizushima S. SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer. Biochem. Biophys. Res. Commun. 174:1991;211-216
80. Driessen A.J.M. SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer. Biochemistry. 32:1993;13190-13197
81. Ding H., Hunt J.F., Mukerji I., Oliver D. Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution. Biochemistry. 42:2003;8729-8738
82. 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. 63:1990;269-279
83. Fekkes P., de Wit J.G., van der Wolk J.P., Kimsey H.H., Kumamoto C.A., Driessen A.J.M. Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA. Mol. Microbiol. 29:1998;1179-1190
84. 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. 16:1997;6105-6113
85. Lill R., Dowhan W., Wickner W. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell. 60:1990;271-280
86. Schiebel E., Driessen A.J.M., Hartl F.U., Wickner W. Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell. 64:1991;927-939
87. 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. 16:1997;7297-7304
88. Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., Deisenhofer J. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science. 297:2002;2018-2026
89. Sharma V., Arockiasamy A., Ronning D.R., Savva C.G., Holzenburg A., Braunstein M., Jacobs W.R. Jr., Sacchettini J.C. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase. Proc. Natl. Acad. Sci. U. S. A. 100:2003;2243-2248
90. Oliver D.B., Cabelli R.J., Dolan K.M., Jarosik G.P. Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc. Natl. Acad. Sci. U. S. A. 87:1990;8227-8231
91. Huie J.L., Silhavy T.J. Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in SecA. J. Bacteriol. 177:1995;3518-3526
92. Schmidt M., Ding H., Ramamurthy V., Mukerji I., Oliver D. Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations. J. Biol. Chem. 275:2000;15440-15448
93. Bolhuis A., Broekhuizen C.P., Sorokin A., van Roosmalen M.L., Venema G., Bron S., Quax W.J., van Dijl J.M. SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. J. Biol. Chem. 273:1998;21217-21224
94. Tseng T.T., Gratwick K.S., Kollman J., Park D., Nies D.H., Goffeau A., Saier M.H. Jr. The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J. Mol. Microbiol. Biotechnol. 1:1999;107-125
95. Kato Y., Nishiyama K., Tokuda H. Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interaction. FEBS Lett. 550:2003;114-118
96. Pogliano J.A., Beckwith J. SecD and SecF facilitate protein export in Escherichia coli. EMBO J. 13:1994;554-561
97. Kim Y.J., Rajapandi T., Oliver D. SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Cell. 78:1994;845-853
98. Economou A., Pogliano J.A., Beckwith J., Oliver D.B., Wickner W. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. Cell. 83:1995;1171-1181
99. Matsuyama S., Fujita Y., Mizushima S. SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli. EMBO J. 12:1993;265-270
100. Saaf A., Monne M., de Gier J.W., von Heijne G. Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli. J. Biol. Chem. 273:1998;30415-30418
101. Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J. Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC. EMBO Rep. 2:2001;524-529
102. van der Laan M., Urbanus M.L., Hagen-Jongman C.M., Nouwen N., Oudega B., Harms N., Driessen A.J.M., Luirink J. A conserved function of YidC in the biogenesis of respiratory chain complexes. Proc. Natl. Acad. Sci. U. S. A. 100:2003;5801-5806
103. Yi L., Jiang F., Chen M., Cain B., Bolhuis A., Dalbey R.E. YidC Is Strictly Required for Membrane Insertion of Subunits a and c of the F(1)F(0)ATP Synthase and SecE of the SecYEG Translocase. Biochemistry. 42:2003;10537-10544
104. Helmers J., Schmidt D., Glavy J.S., Blobel G., Schwartz T. The beta-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the beta-subunit of the signal recognition particle receptor. J. Biol. Chem. 278:2003;23686-23690
105. Finke K., Plath K., Panzner S., Prehn S., Rapoport T.A., Hartmann E., Sommer T. A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J. 15:1996;1482-1494
106. Wilkinson B.M., Tyson J.R., Stirling C.J. Ssh1p determines the translocation and dislocation capacities of the yeast endoplasmic reticulum. Dev. Cell. 1:2001;401-409
107. Robb A., Brown J.D. Protein transport: two translocons are better than one. Mol. Cell. 8:2001;484-486
108. Douglas S.E. A secY homologue is found in the plastid genome of Cryptomonas phi. FEBS Lett. 298:1992;93-96
109. Flachmann R., Michalowski C.B., Loffelhardt W., Bohnert H.J. SecY, an integral subunit of the bacterial preprotein translocase, is encoded by a plastid genome. J. Biol. Chem. 268:1993;7514-7519
110. Vogel H., Fischer S., Valentin K. A model for the evolution of the plastid sec apparatus inferred from secY gene phylogeny. Plant Mol. Biol. 32:1996;685-692
111. Burger G., Lang B.F. Parallels in genome evolution in mitochondria and bacterial symbionts, IUBMB. Life. 55:2003;205-212
112. Kihara A., Akiyama Y., Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. U. S. A. 92:1995;4532-4536
113. Taura T., Baba T., Akiyama Y., Ito K. Determinants of the quantity of the stable SecY complex in the Escherichia coli cell. J. Bacteriol. 175:1993;7771-7775
114. Joly J.C., Leonard M.R., Wickner W.T. Subunit dynamics in Escherichia coli preprotein translocase. Proc. Natl. Acad. Sci. U. S. A. 91:1994;4703-4707
115. Swaving J., van Wely K.H., Driessen A.J.M. Preprotein Translocation by a Hybrid Translocase Composed of Escherichia coli and Bacillus subtilis subunits. J. Bacteriol. 181:1999;7021-7027
116. Baba T., Taura T., Shimoike T., Akiyama Y., Yoshihisa T., Ito K. A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex. Proc. Natl. Acad. Sci. U. S. A. 91:1994;4539-4543
117. Homma T., Yoshihisa T., Ito K. Subunit interactions in the Escherichia coli protein translocase: SecE and SecG associate independently with SecY. FEBS Lett. 408:1997;11-15
118. Mori H., Akiyama Y., Ito K. A SecE mutation that modulates secY-secE translocase assembly, identified as a specific suppressor of SecY defects. J. Bacteriol. 185:2003;948-956
119. Katz B.A., Kossiakoff A. The crystallographically determined structures of atypical strained disulfides engineered into subtilisin. J. Biol. Chem. 261:1986;15480-15485
120. Hazes B., Dijkstra B.W. Model building of disulfide bonds in proteins with known three-dimensional structure. Protein Eng. 2:1988;119-125
121. Satoh Y., Mori H., Ito K. Nearest neighbor analysis of the SecYEG complex. 2. Identification of a SecY-SecE cytosolic interface. Biochemistry. 42:2003;7442-7447
122. Flower A.M., Osborne R.S., Silhavy T.J. The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE. EMBO J. 14:1995;884-893
123. Harris C.R., Silhavy T.J. Mapping an Interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking. J. Bacteriol. 181:1999;3438-3444
124. Kaufmann A., Manting E.H., Veenendaal A.K.J., Driessen A.J.M., van der Does C. Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighboring SecE. Biochemistry. 38:1999;9115-9125
125. Veenendaal A.K.J., van der Does C., Driessen A.J.M. Mapping the Sites of Interaction between SecY and SecE by Cysteine Scanning Mutagenesis. J. Biol. Chem. 276:2001;32559-32566
126. Veenendaal A.K.J., van der Does C., Driessen A.J.M. The core of the bacterial translocase harbors a tilted transmembrane segment 3 of SecE. J. Biol. Chem. 277:2002;36640-36645
127. Breyton C., Haase W., Rapoport T.A., Kuhlbrandt W., Collinson I. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature. 418:2002;662-665
128. van den Berg B., Clemons W.M. Jr., Collinson I., Modis Y., Hartmann E., Harrison S.C., Rapport T.A. X-ray structure of a protein-conducting channel. Nature. 427:2004;36-44
129. Nishiyama K., Mizushima S., Tokuda H. Preferential interaction of Sec-G with Sec-E stabilizes an unstable Sec-E derivative in the Escherichia coli cytoplasmic membrane. Biochem. Biophys. Res. Commun. 217:1995;217-223
130. van der Sluis E., Nouwen N., Driessen A.J.M. SecY-SecY and SecY-SecG contacts revealed by site-specific cross-linking. FEBS Lett. 527:2002;159
131. Satoh Y., Matsumoto G., Mori H., Ito K. Nearest neighbor analysis of the SecYEG complex. 1. Identification of a SecY-SecG interface. Biochemistry. 42:2003;7434-7441
132. Lill R., Cunningham K., Brundage L.A., Ito K., Oliver D., Wickner W. SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli. EMBO J. 8:1989;961-966
133. Natale P., Swaving J., van der Does C., de Keyzer J., Driessen A.J.M. Binding of SecA to the SecYEG complex accelerates the rate of nucleotide exchange on SecA. J. Biol. Chem. 279:2004;13769-13777
134. Manting E.H., van der Does C., Driessen A.J.M. In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase. J. Bacteriol. 179:1997;5699-5704
135. Snyders S., Ramamurthy V., Oliver D. Identification of a region of interaction between Escherichia coli SecA and SecY proteins. J. Biol. Chem. 272:1997;11302-11306
136. Matsumoto G., Yoshihisa T., Ito K. SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane. EMBO J. 16:1997;6384-6393
137. Taura T., Yoshihisa T., Ito K. Protein translocation functions of Escherichia coli SecY: in vitro characterization of cold-sensitive SecY mutants. Biochimie. 79:1997;517-521
138. Mori H., Sugiyama H., Yamanaka M., Sato K., Tagaya M., Mizushima S. Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. J. Biochem. (Tokyo). 124:1998;122-129
139. Hanada M., Nishiyama K., Mizushima S., Tokuda H. Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12). J. Biol. Chem. 269:1994;23625-23631
140. de Keyzer J., van der Does C., Kloosterman T.G., Driessen A.J.M. Direct demonstration of ATP-dependent release of SecA from a translocating preprotein by surface plasmon resonance. J. Biol. Chem. 278:2003;29581-29586
141. Sagara K., Matsuyama S., Mizushima S. SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane. J. Bacteriol. 176:1994;4111-4116
142. Taura T., Akiyama Y., Ito K. Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes. Mol. Gen. Genet. 243:1994;261-269
143. Houben E.N., Scotti P.A., Valent Q.A., Brunner J., de Gier J.L., Oudega B., Luirink J. Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA. FEBS Lett. 476:2000;229-233
144. van der Laan M., Houben E.N., Nouwen N., Luirink J., Driessen A.J.M. Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent manner. EMBO Rep. 2:2001;519-523
145. Beck K., Eisner G., Trescher D., Dalbey R.E., Brunner J., Muller M. 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
146. Urbanus M.L., Froderberg L., Drew D., Bjork P., de Gier J.W., Brunner J., Oudega B., Luirink J. Targeting, insertion, and localization of Escherichia coli YidC. J. Biol. Chem. 277:2002;12718-12723
147. Gorlich D., Prehn S., Hartmann E., Kalies K.U., Rapoport T.A. A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. Cell. 71:1992;489-503
148. Kalies K.U., Gorlich D., Rapoport T.A. Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. J. Cell Biol. 126:1994;925-934
149. Beckmann R., Bubeck D., Grassucci R., Penczek P., Verschoor A., Blobel G., Frank J. Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science. 278:1997;2123-2126
150. Menetret J.F., Neuhof A., Morgan D.G., Plath K., Radermacher M., Rapoport T.A., Akey C.W. The structure of ribosome-channel complexes engaged in protein translocation. Mol. Cell. 6:2000;1219-1232
151. Beckmann R., Spahn C.M., Eswar N., Helmers J., Penczek P.A., Sali A., Frank J., Blobel G. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell. 107:2001;361-372
152. Potter M.D., Nicchitta C.V. Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon following termination of protein synthesis. J. Biol. Chem. 277:2002;23314-23320
153. Joly J.C., Wickner W.T. The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids. EMBO J. 12:1993;255-263
154. Crowley K.S., Liao S., Worrell V.E., Reinhart G.D., Johnson A.E. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell. 78:1994;461-471
155. Plath K., Mothes W., Wilkinson B.M., Stirling C.J., Rapoport T.A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell. 94:1998;795-807
156. Wilkinson B.M., Esnault Y., Craven R.A., Skiba F., Fieschi J., K'epes F., Stirling C.J. Molecular architecture of the ER translocase probed by chemical cross-linking of Sss1p to complementary fragments of Sec61p. EMBO J. 16:1997;4549-4559
157. Hanein D., Matlack K.E., Jungnickel B., Plath K., Kalies K.U., Miller K.R., Rapoport T.A., Akey C.W. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell. 87:1996;721-732
158. van Wely K.H.M., Swaving J., Broekhuizen C.P., Rose M., Quax W.J., Driessen A.J.M. Functional identification of the product of the Bacillus subtilis yvaL gene as a SecG homologue. J. Bacteriol. 181:1999;1786-1792
159. Meyer T.H., Ménétret J.F., Breitling R., Miller K.R., Akey C.W., Rapoport T.A. The Bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex. J. Mol. Biol. 285:1999;1789-1800
160. Manting E.H., van der Does C., Remigy H., Engel A., Driessen A.J.M. SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19:2000;852-861
161. Collinson I., Breyton C., Duong F., Tziatzios C., Schubert D., Or E., Rapoport T., Kuhlbrandt W. Projection structure and oligomeric properties of a bacterial core protein translocase. EMBO J. 20:2001;2462-2471
162. Bessonneau P., Besson V., Collinson I., Duong F. The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure. EMBO J. 21:2002;995-1003
163. Mori H., Tsukazaki T., Masui R., Kuramitsu S., Yokoyama S., Johnson A.E., Kimura Y., Akiyama Y., Ito K. Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes. J. Biol. Chem. 278:2003;14257-14264
164. Duong F. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase. EMBO J. 22:2003;4375-4384
165. Yahr T.L., Wickner W.T. Evaluating the oligomeric state of SecYEG in preprotein translocase. EMBO J. 19:2000;4393-4401
166. Driessen A.J.M., Wickner W. Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocase. Proc. Natl. Acad. Sci. U. S. A. 88:1991;2471-2475
167. 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. 265:1990;17341-17347
168. Tani K., Mizushima S. A chemically cross-linked nonlinear proOmpA molecule can be translocated into everted membrane vesicles of Escherichia coli in the presence of the proton motive force. FEBS Lett. 285:1991;127-131
169. Nouwen N., de Kruijff B., Tommassen J. prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors. Proc. Natl. Acad. Sci. U. S. A. 93:1996;5953-5957
170. de Keyzer J., van der Does C., Driessen A.J.M. Kinetic analysis of the translocation of fluorescent precursor proteins into Escherichia coli membrane vesicles. J. Biol. Chem. 277:2002;46059-46065
171. Duong F., Wickner W. The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits. EMBO J. 18:1999;3263-3270
172. Mori H., Shimizu Y., Ito K. Superactive SecY variants that fulfill the essential translocation function with a reduced cellular quantity. J. Biol. Chem. 277:2002;48550-48557
173. Manting E.H., Kaufmann A., van der Does C., Driessen A.J.M. A Single Amino Acid Substitution in SecY Stabilizes the Interaction with SecA. J. Biol. Chem. 274:1999;23868-23874
174. Matsuyama S., Akimaru J., Mizushima S. SecE-dependent overproduction of SecY in Escherichia coli. Evidence for interaction between two components of the secretory machinery. FEBS Lett. 269:1990;96-100
175. Hamman B.D., Chen J.C., Johnson E.E., Johnson A.E. The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane. Cell. 89:1997;535-544
176. Wirth A., Jung M., Bies C., Frien M., Tyedmers J., Zimmermann R., Wagner R. The Sec61p complex is a dynamic precursor activated channel. Mol. Cell. 12:2003;261-268
177. de Keyzer J., van der Does C., Swaving J., Driessen A.J.M. The F286Y mutation of PrlA4 tempers the signal sequence suppressor phenotype by reducing the SecA binding affinity. FEBS Lett. 510:2002;17-21