Document Detail


Short hydrophobic segments in the mature domain of ProOmpA determine its stepwise movement during translocation across the cytoplasmic membrane of Escherichia coli.
MedLine Citation:
PMID:  9038205     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Based on the finding that a series of engineered proOmpAs containing disulfide-bridged loops of different sizes at different positions exhibits a discontinuous mode of polypeptide transit across the cytoplasmic membrane of Escherichia coli, we suggested previously that the translocation of preproteins takes place at every 30 amino acid residues (Uchida, K., Mori, H., and Mizushima, S. (1995) J. Biol. Chem. 270, 30862-30868). In the present study, we investigated the molecular mechanism underlying this stepwise translocation. Deletion or relocation of hydrophobic segments of the mature domain of proOmpA (H1, residues 233-237; H2, residues 261-265) significantly altered the pattern of the stepwise translocation. The stepwise mode of polypeptide insertion was also observed with reconstituted proteoliposomes comprising purified SecA, SecY, and SecE. Cross-linking experiments involving a photoactivable cross-linker revealed that SecY and SecA are the components which interact with the hydrophobic segment of proOmpA. The present results indicate that the hydrophobic segments of the mature domains of preproteins interact with membrane embedded translocase during polypeptide transit across the membrane, which causes a discontinuous mode of polypeptide movement.
Authors:
K Sato; H Mori; M Yoshida; M Tagaya; S Mizushima
Related Documents :
16221685 - A prohormone convertase cleavage site within a predicted alpha-helix mediates sorting o...
11906185 - Purification and characterization of two active derivatives of recombinant ypla, a secr...
1760845 - The essential tyrosine of the internalization signal in lysosomal acid phosphatase is p...
9038205 - Short hydrophobic segments in the mature domain of proompa determine its stepwise movem...
25402195 - Mapping the accessibility of the disulfide crosslink network in the wool fibre cortex.
12763315 - Specific recognition of primer trna lys 3 by hiv-1 nucleocapsid protein: involvement of...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  272     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1997 Feb 
Date Detail:
Created Date:  1997-04-15     Completed Date:  1997-04-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5880-6     Citation Subset:  IM    
Affiliation:
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / metabolism
Bacterial Outer Membrane Proteins / chemistry*
Bacterial Proteins / metabolism
Biological Transport
Cell Membrane / metabolism*
Endopeptidase K / metabolism
Escherichia coli
Escherichia coli Proteins*
Membrane Transport Proteins*
Protein Conformation
Protein Precursors / chemistry*
Chemical
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Membrane Transport Proteins; 0/Protein Precursors; 0/outer membrane protein A precursor (E coli); 119129-39-4/SecA protein, Bacteria; EC 3.4.21.64/Endopeptidase K; EC 3.6.1.-/Adenosine Triphosphatases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Role of positive and negative cis-regulatory elements in the transcriptional activation of the lysoz...
Next Document:  Casein kinase II binds to and phosphorylates cytoplasmic dynein.