Document Detail


Reconstitution of functionally efficient SecA-dependent protein-conducting channels: transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels.
MedLine Citation:
PMID:  23337498     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Previous work showed that SecA alone can promote protein translocation and ion-channel activity in liposomes, and that SecYEG increases efficiency as well as signal peptide specificity. We now report that SecDF·YajC further increases translocation and ion-channel activity. These activities of reconstituted SecA-SecYEG-SecDF·YajC-liposome are almost the same as those of native membranes, indicating the transformation of reconstituted functional high-affinity protein-conducting channels from the low-affinity SecA-channels.
Authors:
Ying-hsin Hsieh; Hao Zhang; Hongyun Wang; Hsiuchin Yang; Chun Jiang; Sen-fang Sui; Phang C Tai
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-01-18
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  431     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-18     Completed Date:  2013-08-27     Revised Date:  2014-09-21    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  388-92     Citation Subset:  IM    
Copyright Information:
Published by Elsevier Inc.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / chemistry,  metabolism*
Animals
Bacterial Proteins / chemistry,  metabolism*
Escherichia coli Proteins / chemistry,  metabolism*
Ion Channels / chemistry,  metabolism*
Liposomes / chemistry,  metabolism*
Membrane Proteins / chemistry,  metabolism*
Membrane Transport Proteins / chemistry,  metabolism*
Protein Transport
Xenopus laevis
Grant Support
ID/Acronym/Agency:
R01 NS073875/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Ion Channels; 0/Liposomes; 0/Membrane Proteins; 0/Membrane Transport Proteins; 0/SecD protein, E coli; 0/SecF protein, E coli; 0/SecYEG protein, E coli; 119129-39-4/SecA protein, Bacteria; EC 3.6.1.-/Adenosine Triphosphatases

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


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