The Sec system

Current Opinion in Microbiology

Volumn 1, Issue 2, 1998, Pages 216-222

  Driessen, Arnold J M ^a   Fekkes, Peter ^a   Van Der Wolk, Jeroen P W ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CARRIER PROTEIN; CHAPERONE; ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; SECA PROTEIN, BACTERIA; SECB PROTEIN, BACTERIA; SIGNAL PEPTIDE;

CELL MEMBRANE; ESCHERICHIA COLI; GENETICS; METABOLISM; REVIEW; TRANSPORT AT THE CELLULAR LEVEL;

ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; CELL MEMBRANE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MOLECULAR CHAPERONES; PROTEIN SORTING SIGNALS;

EID: 0032035297     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(98)80014-3     Document Type: Article

References (49)

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13. •,26], the region may have altered its location at the initiation of translocation.
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17. Manting EH, van der Does C, Driessen AJM: SecA and SecY are associated subunits of the Escherichia coli precursor protein translocase. J Bacteriol 1997, 179:5699-5704.
18. Matsumoto G, Yoshihisa T, Ho K: SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane. EMBO J 1997, 16:6384-6393.
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20. Mitchell C, Oliver D: Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mol Microbiol 1993, 10:483-497.
21. Economou A, Pogliano JA, Beckwith J, Oliver DB, Wickner W: SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. Cell 1995, 83:1171-1181.
22. Den Blaauwen T, Fekkes P, De Wit JG, Kuiper W, Driessen AJM: Domain interactions of the peripheral preprotein translocase subunit SecA. Biochemistry 1996, 35:11994-12004. The authors report on the SecA domain organization and show thai SecA consists of at least two domains that interact in a nucleotide-dependent manner. The data indicate that SecA functions as a molecular motor.
23. Ramamurthy V, Oliver D: Topology of integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding. J Biol Chem 1997, 272:23239-23246. A clear demonstration, by the use of membrane-impermeable cysteine-reactive agents and single cysteine mutants of SecA, that various regions of the membrane-integrated form of SecA are accessible from the periplasmic face of the membrane, thus indicating a complex topology.
24. Van der Wolk JPW, Boorsma A, Knoche M, Schäfer H-J, Driessen AJM: The low affinity ATP-binding site of the Escherichia coli SecA dimer is localized at the subunit interface. Biochemistry 1997, 36:14924-14929
25. Hirano M, Matsuyama S, Tokuda H: The carboxyl-terminal region is essential for SecA dimerization. Biochem Biophys Res Commun 1996, 229:90-95.
26. Van der Does C, Den Blaauwen T, De Wit JG, Manting EH, Groot NA, Fekkes P, Driessen AJM: SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxy-terminus to the periplasm. Mol Microbiol 1996, 22:619-629.
27. Economou A, Wickner W: SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 1994, 78:835-843.
28. Douville K, Price A, Eichler J, Economou A, Wickner W: SecYEG and SecA are the stoichiometric components of preprotein translocase. J Biol Chem 1995, 270:20106-20111.
29. Price A, Economou A, Duong F, Wickner W: Separable ATPase and membrane insertion domains of the SecA subunit of preprotein translocase. J Biol Chem 1996, 271:31580-31584.
30. Chen X, Xu H, Tai PC: A significant fraction of functional SecA Is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation. J Biol Chem 1996, 271:29698-29706.
31. Eichler J, Wickner W: Both an N-terminal 65 kDa domain and a C-terminal 30 kDa domain of SecA cycle into the membrane at SecYEG during translocation. Proc Natl Acad Sci USA 1997, 94:5574-5581.
32. Eichler J, Brunner J, Wickner W: The protease-protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase. EMBO J 1997, 16:2188-2196. Tests the hypothesis that the 30 kDa domain of SecA is membrane-integrated by probing its localization by means of a photoaffinity crosslinking lipid analog. The 30 kDa domain is shielded from the lipid phase and presumably present in an aqueous or proteaceous environment.
33. Den Blaauwen T, De Wit JG, Gosker H, Van der Does C, Breukink E, De Leij L, Driessen AJM: Inhibition of preprotein translocation and reversion of the membrane inserted state of SecA by a carboxyl terminus binding mAb. Biochemistry 1997, 36:9159-9168.
34. •] and further show that the 30 kDa SecA fragment is also not protected by the SecYEG protein. It is concluded that this SecA fragment represents a stable conformation of a pre-existing domain.
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36. H+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 1991, 64:927-939.
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38. Huie JL, Silhavy TJ: Suppression of signal sequence defects and azide resistance in Escherichia coli commonly results from the same mutations in secA J Bacteriol 1995, 177:3518-3526.
39. Osborne RS, Silhavy TJ: PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains. BMBO J 1993, 12:3391-3398.
40. 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 USA 1996, 93:5953-5957. Shows that, in a prlA mutant strain, preprotein translocation exhibits a reduced protonmotive force requirement.
41. Van der Wolk JPW, De Wit JG, Driessen AJM: The catalytic cycle of the Escherichia colt SecA ATPase comprises two distinct preprotein translocation events. EMBO J 1997, 16:7297-7304. This paper demonstrates that a catalytic preprotein translocation cycle of SecA consists of two distinct translocation steps. Each of these steps allows the translocation of ∼20-25 amino acyl residues of the SecA-bound preprotein. One step is driven by the binding of SecA to the translocating pclypeptide chain and the other step is driven by the binding of ATP to SecA.
42. Uchida K, Mori H, Mizushima M: Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. J Biol Chem 1995, 270:30862-30868.
43. 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 1994, 13:3272-3277.
44. Pogliano JA, Beckwith J: SecD and SecF facilitate protein export in Escherichia coli. EMBO J 1994, 13:554-561.
45. Nishiyama KI, Suzuki T, Tokuda H: Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell 1996, 85:71-81. This is an excellent paper showing that SecG undergoes a remarkable membrane topology inversion when SecA binds ATP.
46. Arkowitz RA, Wickner W: SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation. EMBO J 1994, 13:954-963.
47. Duong F, Wickner W: The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling. EMBO J 1997, 16:4871-4379. This paper demonstrates that SecD and SecF prevent the backward sliding of a translocating polypeptide chain and, together with Economou et al., 1995 [21], shows that SecD and SecF stabilize the 30 kDa SecA domain.
48. Hanein D, Matlack KE, Jungnickel B, Plath K, Kalies KU, Miller KR, Rapoport TA, Akey CW: Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 1996, 87:535-544. This is the first low-resolution structural information on a preprotein translocation pore, showing ring-like structures with a central pore-like opening. As the SecYEG complex as has a similar function and subunit organization to the endoplasmic reticulum Sec61p, it is probable that the bacterial translocase has a similar overall structure.
49. Rietveld AG, Koorengevel, MC, de Kruijff B: Non-bilayer lipids are required for efficient protein transport across the plasma membrane of Escherichia coli. EMBO J 1995, 14:5506-5513.