The structural basis of protein targeting and translocation in bacteria

Nature Structural Biology

Volumn 8, Issue 6, 2001, Pages 492-498

  Driessen, Arnold J M ^a   Manting, Erik H ^a,b   Van Der Does, Chris ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b Sanquin CLB ^*  (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CARRIER PROTEIN; CHAPERONE; CYTOPLASM PROTEIN; MEMBRANE PROTEIN; PROTEIN SECA; PROTEIN SECB; SIGNAL RECOGNITION PARTICLE; UNCLASSIFIED DRUG;

BACTERIAL MEMBRANE; BACTERIAL TRANSLOCATION; GRAM NEGATIVE BACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTEIN TARGETING; REVIEW; RIBOSOME; STRUCTURE ANALYSIS;

ADENOSINE TRIPHOSPHATASES; BACTERIA; BACTERIAL PROTEINS; CARRIER PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN PRECURSORS; PROTEIN TRANSPORT; RIBOSOMES; SIGNAL RECOGNITION PARTICLE;

EID: 0034995184     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/88549     Document Type: Review

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4. The Escherichia coli SRP and SecB targeting pathways converge at the translocon
5. Escherichia coli translocase: The unraveling of a molecular machine
6. Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
7. YidC, the Escherichia coli homologue of mitochondrial Oxa 1p, is a component of the Sec translocase
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9. Evolutionary conservation of components of the protein translocation complex
10. The translocon: A dynamic gateway at the ER membrane
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14. Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
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19. Crystal structure of the signal sequence binding subunit of the signal recognition particle
20. 2+GDP
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22. Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
23. The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain
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33. Determination of the binding frame within a physiological ligand for the chaperone SecB
34. Preprotein transfer to the Escherichia coli translocase requires the cooperative binding of SecB and the signal sequence to SecA
35. Membrane vesicles containing overproduced SecY and SecE exhibit high translocation ATPase activity and countermovement of protons in a SecA- and presecretory protein-dependent manner
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37. Translocase-bound SecA is largely shielded from the phospholipid acyl chains
38. ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase
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40. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
41. Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighboring SecE
42. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation
43. Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex
44. The structure of ribosome-channel complexes engaged in protein translocation
45. The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex
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47. Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization
48. SecYEG assembles into a tetramer to form the active protein translocation channel
49. A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
50. Two independent mechanisms down-regulate the intrinsic SecA ATPase activity
51. Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation
52. Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding
53. Interaction between SecA and SecYEG in micellar solution and formation of the membrane-inserted state
54. Escherichia coli SecA shape and dimensions
55. Evaluating the oligomeric state of SecYEG in preprotein translocase