Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane

EMBO Journal

Volumn 21, Issue 17, 2002, Pages 4470-4479

  Or, Eran ^a   Navon, Amiel ^a   Rapoport, Tom ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

FRET; Helicases; Monomer; SecA; Translocation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HELICASE; PEPTIDE; PHOSPHOLIPID; PROTEIN; PROTEIN SECA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; DISSOCIATION; ENZYME ANALYSIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN TRANSPORT;

ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; CELL MEMBRANE; DETERGENTS; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUCOSIDES; LIPOSOMES; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLETHANOLAMINES; PROTEIN PRECURSORS; PROTEIN SORTING SIGNALS; PROTEIN TRANSPORT; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS);

EID: 0037009514     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf471     Document Type: Article

References (51)

1. SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer
2. Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli
3. Projection structure and oligomeric properties of a bacterial core protein translocase
4. ProOmpA is stabilized for membrane translocation by either purified E.coli trigger factor or canine signal recognition particle
5. Specifc recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli
6. Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membrane
7. The ATPase domain of SecA can form a tetramer in solution
8. Characterization of Escherichia coli SecA protein binding to a site on its mRNA involved in autoregulation
9. SecA folds via a dimeric intermediate
10. Precursor protein translocation by the Escherichia coli translocase is directed by the protonmotive force
11. SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
12. Distinct catalyic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
13. The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits
14. Biogenesis of the Gram-negative bacterial envelope
15. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
16. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
17. Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: Evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes
18. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E.coli plasma membrane
19. The carboxyl-terminal region is essential for SecA dimerization
20. A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
21. Hepatitis C virus NS3 helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
22. Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein
23. Major domain swiveling revealed by the crystal structures of complexes of E.coli Rep helicase bound to single-stranded DNA and ADP
24. Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membranes
25. The ATPase activity of SecA is regulated by acidic phospholipids, SecY and the leader and mature domains of precursor proteins
26. Escherichia coli translocase: The unravelling of a molecular machine
27. BiP acts as a molecular ratchet in posttranslational protein transport across the ER membrane
28. Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region
29. Site-directed cross-linking
30. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
31. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
32. RNA helicase activity of Escherichia coli SecA protein
33. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
34. SecD and SecF facilitate protein export in Escherichia coli
35. Protein translocation in the three domains of life: Variation on a theme
36. The first gene in the Escherichia coli secA operon, gene X, encodes a nonessential secretory protein
37. Localization of the elongation factor Tu binding site on Escherichia coli ribosomes
38. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
39. H+ and ATP function at different steps of the catalytic cycle of preprotein translocase
40. Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation
41. The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles and phospholipids
42. Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function
43. Structural mapping of chloroplast coupling factor
44. DNA helicases: 'Inching forward'
45. Increases in acidic phospholipid contents specifically restore protein translocation in a cold-sensitive secA or secG null mutant
46. Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity
47. Deep penentration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding
48. Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase
49. PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation
50. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
51. Complex behavior in solution of homodimeric SecA