SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion

Cell

Volumn 78, Issue 5, 1994, Pages 835-843

  Economou, Anastassios ^a   Wickner, William ^a  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; LIPOSOME; MEMBRANE PROTEIN; PROTEIN PRECURSOR;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; ESCHERICHIA COLI; MEMBRANE TRANSPORT; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN TRANSPORT; PROTON TRANSPORT; SIGNAL TRANSDUCTION;

ESCHERICHIA COLI;

EID: 0028064967     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(94)90582-7     Document Type: Article

References (54)

1. SecA an essential component of the secretory machinery of Escherichia coli exists as a homodimer
2. Translocation can drive the unfolding of a preprotein domain
3. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface
4. Purified E coli preprotein translocase catalyzes multiple cycles of precursor protein translocation
5. SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP a monolayer study
6. The purified E coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation
7. SecY SecE and Band 1 form the membrane-embedded domain of E coli preprotein translocase
8. Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(Ts) mutant strains of Escherichia coli
9. Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction endoproteolytic cleavage of nascent f1 pre-coat protein
10. Roles of H+-ATPase and proton motive force in ATP-dependent protein translocation in vitro
11. ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes
12. Isolation of SecA protein a peripheral protein of the E coli plasma membrane that is essential for the functional binding and translocation of proOmpA
13. Role for membrane potential in the secretion of protein into the periplasm of Escherichia coli
14. The effects of energy poisons on the conversion of soluble M13 procoat to membrane-bound coat protein
15. A signal sequence is not required for protein export in prlA mutants of Escherichia coli
16. Characterization of Escherichia coli SecA protein binding to a site on its own mRNA involved in autoregulation
17. The band 1 subunit of Escherichia coli preprotein translocase and the integral membrane export factor P12 are the same protein
18. SecA the peripheral subunit of the Escherichia coli precursor protein translocase is functional as a dimer
19. Energy is required for maturation of exported proteins in Escherichia coli
20. SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles
21. Novel SecA alleles improve export of maltose-binding protein synthesized with a defective signal peptide
22. secD, a new gene involved in protein export in Escherichia coli
23. Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles
24. The binding of SecB to SecA to SecY/E mediates preprotein targeting to the E coli membrane
25. SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the E coli plasma membrane
26. Synthesis assembly into the cytoplasmic membrane and proteolytic processing of the precursor of coliphage M13 coat protein
27. The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein shielding it from phospholipids
28. Membrane vesicles containing overproduced SecY and SecE exhibit high translocation ATPase activity and countermovement of protons in a SecA- and presecretory protein-dependent manner
29. Identification of the histidine permease HisQMP complex
30. SecA protein is exposed to the periplasmic surface of the E coli inner membrane in its active state
31. In vivo evidence for the role of the ɛ subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
32. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
33. Escherichia coli SecB protein associates with exported protein precursor in vivo
34. Three pure chaperone proteins of Escherichia coli SecB trigger factor and GroEL form soluble complexes with precursor proteins in vitro
35. The SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of E coli
36. The ATPase activity of SecA is regulated by acidic phospholipids SecY and the leader and mature domains of precursor proteins
37. Surface specific iodination of membrane proteins of viruses and eukaryotic cells using 1346-tetrachloro-3α6α-diphenylglycouril
38. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
39. A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli
40. SecA protein autoregulated ATPase catalyzing preprotein insertion and translocation across the Escherichia coli inner membrane
41. SecA protein autoregulated initiator of secretory precursor protein translocation across the E coli plasma membrane
42. Regulation of the Escherichia coli secA gene by protein secretion defects analysis of secA secB secD and secY mutants
43. The attractions of proteins for small molecules and ions
44. Preprotein translocation creates a halide anion permeability in the Escherichia coli plasma membrane
45. H+ and ATP function at different steps of the catalytic cycle of preprotein translocase
46. Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli
47. The conformation of SecA as revealed by its protease sensitivity is altered upon interaction with ATP presecretory proteins everted membrane vesicles and phospholipids
48. The proton motive force lowers the level of ATP required for the in vitro translocation of a secretory protein in Escherichia coli
49. In vitro analysis of the process of translocation of OmpA across the Escherichia coli cytoplasmic membrane
50. Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic lipids and by partial unfolding
51. Electron microscopy of thin-sectioned three-dimensional crystals of SecA protein from Escherichia coli structure in projection at 40 resolution
52. The enzymology of protein translocation across the Escherichia coli plasma membrane
53. Purification and characterization of leader peptidase from E coli
54. A high concentration of SecA allows proton motive force-independent translocation of a model secretory protein in Escherichia coli membrane vesicles