Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum

Molecular and Cellular Biology

Volumn 20, Issue 18, 2000, Pages 6923-6934

  Kabani, M ^a   Beckerich, J M ^a   Gaillardin, C ^a  

^a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; CHAPERONE; DNA; SIGNAL RECOGNITION PARTICLE;

ARTICLE; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; YARROWIA LIPOLYTICA; YEAST;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; CARRIER PROTEINS; CATTLE; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; GLUTATHIONE TRANSFERASE; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN BINDING; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 0033811675     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.18.6923-6934.2000     Document Type: Article

References (69)

1. Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex
2. A homologue of the bacterial heatshock gene DnaJ that alters protein sorting in yeast
3. A mutation in the secretion pathway of the yeast Yarrowia lipolytica that displays synthetic lethality in combination with a mutation affecting the signal recognition particle
4. Sls1p, an endoplasmic reticulum component, is involved in the protein translocation process in the yeast Yarrowia lipolytica
5. Interaction of Kar2p and Sls1p is required for efficient co-translational translocation of secreted proteins in the yeast Yarrowia lipolytica
6. Identification of an essential Schizosaccharomyces pombe RNA homologous to the 7SL component of signal recognition particle
7. BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum
8. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
9. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
10. The ATPase core of a clathrin uncoating protein
11. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae
12. Mechanism of polypeptide translocation into the endoplasmic reticulum
13. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
14. Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
15. Detection of transient in vivo interactions between substrate and transporter during protein translocation into the endoplasmic reticulum
16. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation
17. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
18. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone
19. Role and regulation of the ER chaperone BiP
20. Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
21. Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
22. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
23. SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling
24. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
25. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation
26. The signal recognition particle in S. cerevisiae
27. The yeast Yarrowia lipolytica has two, functional, signal recognition particle 7S RNA genes
28. Protein translocation at the membrane of the endoplasmic reticulum
29. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
30. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
31. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
32. The translocon: A dynamic gateway at the ER membrane
33. A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica
34. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway
35. A rapid permeabilization procedure for accurate quantitative determination of beta-galactosidase activity in yeast cells
36. Rapid and efficient site-specific mutagenesis without phenotypic selection
37. Yarrowia lipolytica SRP54 homolog and translocation of Kar2p
38. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
39. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
40. Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae
41. The TSR1 gene of Yarrowia lipolytica is involved in the signal recognition particle-dependent translocation pathway of secretory proteins
42. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
43. Protein transport by purified yeast Sec complex and Kar2p without membranes
44. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER
45. Mgel functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
46. Mutational analysis of the human HSP70 protein: Distinct domains for nucleolar localization and adenosine triphosphate binding
47. Complementation of saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs
48. Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex
49. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
50. Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae
51. ER membrane protein complex required for nuclear fusion
52. The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion
53. + but not ATP hydrolysis
54. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
55. ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
56. Posttranslational protein translocation across the membrane of the endoplasmic reticulum
57. Approaching the mechanism of protein transport across the ER membrane
58. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
59. A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein
60. Isolation and cloning of the Yarrowia lipolytica SEC65 gene, a component of the yeast signal recognition particle displaying homology with the human SRP19 gene
61. Kinetics of molecular chaperone action
62. Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum
63. A prepriming DNA replication enzyme of Escherichia coli I. Purification of protein n': A sequence-specific, DNA-dependent ATPase
64. A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum
65. A protein-conducting channel in the endoplasmic reticulum
66. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
67. In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis
68. Structural analysis of substrate binding by the molecular chaperone DnaK