Document Detail

YidC protein, a molecular chaperone for LacY protein folding via the SecYEG protein machinery.
MedLine Citation:
PMID:  23928306     Owner:  NLM     Status:  MEDLINE    
To understand how YidC and SecYEG function together in membrane protein topogenesis, insertion and folding of the lactose permease of Escherichia coli (LacY), a 12-transmembrane helix protein LacY that catalyzes symport of a galactoside and an H(+), was studied. Although both the SecYEG machinery and signal recognition particle are required for insertion of LacY into the membrane, YidC is not required for translocation of the six periplasmic loops in LacY. Rather, YidC acts as a chaperone, facilitating LacY folding. Upon YidC depletion, the conformation of LacY is perturbed, as judged by monoclonal antibody binding studies and by in vivo cross-linking between introduced Cys pairs. Disulfide cross-linking also demonstrates that YidC interacts with multiple transmembrane segments of LacY during membrane biogenesis. Moreover, YidC is strictly required for insertion of M13 procoat protein fused into the middle cytoplasmic loop of LacY. In contrast, the loops preceding and following the inserted procoat domain are dependent on SecYEG for insertion. These studies demonstrate close cooperation between the two complexes in membrane biogenesis and that YidC functions primarily as a foldase for LacY.
Lu Zhu; H Ronald Kaback; Ross E Dalbey
Related Documents :
16656626 - Relationship between protein synthesis in tuber discs and the protein synthetic activit...
23341326 - Mitochondrial protein homeostasis.
25108686 - Visualizing a protein quake with time-resolved x-ray scattering at a free-electron laser.
24553416 - Antigenic proteins of flavobacterium psychrophilum recognized by ayu plecoglossus altiv...
16619306 - Depletion of abundant proteins from non-human primate serum for biomarker studies.
9261676 - Quantitative comparison of shear-dependent staphylococcus aureus adhesion to three poly...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2013-08-08
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 Sep 
Date Detail:
Created Date:  2013-09-30     Completed Date:  2013-12-24     Revised Date:  2014-09-30    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  28180-94     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Disulfides / chemistry
Escherichia coli / enzymology*
Escherichia coli Proteins / metabolism*
Membrane Proteins / metabolism*
Membrane Transport Proteins / metabolism*
Models, Molecular
Molecular Chaperones / metabolism
Monosaccharide Transport Proteins / metabolism*
Mutagenesis, Site-Directed
Peptide Hydrolases / chemistry
Protein Binding
Protein Folding
Protein Structure, Tertiary
Symporters / metabolism*
Grant Support
Reg. No./Substance:
0/Disulfides; 0/Escherichia coli Proteins; 0/LacY protein, E coli; 0/Membrane Proteins; 0/Membrane Transport Proteins; 0/Molecular Chaperones; 0/Monosaccharide Transport Proteins; 0/SecE protein, E coli; 0/SecG protein, E coli; 0/SecY protein, E coli; 0/Symporters; 0/YIDC protein, E coli; EC 3.4.-/Peptide Hydrolases

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

Previous Document:  The malignant brain tumor (MBT) domain protein SFMBT1 is an integral histone reader subunit of the L...
Next Document:  Complement-mediated opsonization of invasive group A Streptococcus pyogenes strain AP53 is regulated...