Sec-dependent protein export and the involvement of the molecular chaperone SecB

Cell Stress and Chaperones

Volumn 5, Issue 4, 2000, Pages 267-275

  Kim, J ^a   Kendall, D A ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL RNA; CHAPERONE; PROTEIN SECB; SIGNAL RECOGNITION PARTICLE; UNCLASSIFIED DRUG;

ESCHERICHIA COLI; MEMBRANE TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECRETION; PROTEIN TRANSPORT; REVIEW; SITE DIRECTED MUTAGENESIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033669317     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2000)005<0267:SDPEAT>2.0.CO;2     Document Type: Review

References (82)

1. Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein
2. The presence of both the signal sequence and a region of mature Lamb protein is required for the interaction of Lamb with the export factor SecB
3. Purified Escherichia coli preprotein translocase catalyzes multiple cycles of precursor protein translocation
4. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
5. Transfer of proteins across membranes
6. Transient association of newly synthesized unfolded proteins with the heatshock GroEL protein
7. Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coli
8. The GTPase superfamily: Conserved structure and molecular mechanism
9. SecY, SecE and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase
10. The purified E coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation
11. SecA protein is required for secretory protein translocation into E coli membrane vesicles
12. Evidence for the involvement of ATP co-translational protein translocation
13. Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 Å resolution: Evidence for the mechanism of signal peptide binding
14. The antifolding activity of SecB promotes the export of the E coli maltose-binding protein
15. The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide
16. ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes
17. SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA
18. Inhibition of PhoE translocation across Escherichia coli inner-membrane vesicles by synthetic signal peptides suggests an important role of acidic phospholipids in protein translocation
19. Kinetic partitioning
20. Band 1 subunit of preprotein translocase and integral membrane export factor P12 are the same protein
21. SecYEG are the stoichiometric components of preprotein translocase
22. SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
23. Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
24. The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
25. Preprotein transfer to the Escherichia coli translocase requires the cooperative binding of SecB and the signal sequence to SecA
26. Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB
27. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
28. Structure of the conserved GTPase domain of the signal recognition particle
29. The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export
30. Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12)
31. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation
32. A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB
33. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E coli plasma membrane
34. Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system
35. Secretion and membrane localization of proteins in Escherichia coli
36. Physical and conformational properties of synthetic idealized signal sequences parallel their biological function
37. Subunit dynamics in Escherichia coli preprotein translocase
38. Biophysical studies of signal peptides: Implications for signal sequence functions and the involvement of lipid in protein export
39. Crystal structure of the signal sequence binding subunit of the signal recognition particle
40. SecB dependence of an exported protein is a continuum influenced by the characteristics of the signal peptide or early mature region
41. Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB
42. Substrate specificity of the SecB chaperone
43. Escherichia coli SecB protein associates with exported protein precursors in vivo
44. SecB protein: A cytosolic export factor that associates with nascent exported proteins
45. Molecular chaperones and protein translocation across the Escherichia coli inner membrane
46. Mutations in a new gene, secB, cause defective protein localization in Escherichia coli
47. Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics
48. Characterization of the Escherichia coli protein-export gene secB
49. SecB protein stabilizes a translocation-competent state of purified prePhoE protein
50. SRP-RNA sequence alignment and secondary structure
51. Three pure chaperone proteins of Escherichia coli - SecB, trigger factor and GroEL - Form soluble complexes with precursor proteins in vitro
52. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
53. An alternative protein targeting pathway in Escherichia coli: Studies on the role of FtsY
54. The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex
55. Synthetic signal peptides specifically recognize SecA and stimulate ATPase activity in the absence of preprotein
56. Interaction of E coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor
57. Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
58. 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
59. A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli
60. The E coli ffh gene is necessary for viability and efficient protein export
61. An E coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle
62. Human SRP RNA and E coli 4.5S RNA contain a highly homologous domain
63. Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo
64. Peptide binding by chaperone SecB: Implications for recognition of nonnative structure
65. Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E coli
66. No specific recognition of leader peptide by SecB, a chaperone involved in protein export
67. The basis of recognition of nonnative structure by the chaperone SecB
68. E coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle
69. GTPase domain of the 54-kD subunit of the mammalian signal recognition particle is required for protein translocation but not for signal sequence binding
70. The secE gene encodes an integral membrane protein required for protein export in Escherichia coli
71. A protein-conducting channel in the endoplasmic reticulum
72. Signal peptides open protein-conducting channels in E coli
73. Determination of the binding frame within a physiological ligand for the chaperone SecB
74. Early events in preprotein recognition in E coli: Interaction of SRP and trigger factor with nascent polypeptides
75. The Escherichia coli SRP and SecB targeting pathways converge at the translocon
76. Trans-membrane translocation of proteins
77. Signal sequence recognition and protein targeting to the endoplasmic reticulum
78. Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB
79. Synthesis and export of the outer membrane lipoprotein in Escherichia coli mutants defective in generalized protein export
80. Purified SecB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro
81. Domain interactions in E coli SRP: Stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain
82. The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain