Document Detail


Subunit proximity in the H+-translocating NADH-quinone oxidoreductase probed by zero-length cross-linking.
MedLine Citation:
PMID:  15035646     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans is composed of 14 different subunits (designated Nqo1-14), seven of which are located in the membrane domain and the other seven in the peripheral domain. It has been previously reported that membrane domain subunit Nqo7 (ND3) directly interacts with peripheral subunit Nqo6 (PSST) by using a cross-linker, m-maleimidobenzoyl-N-hydrosuccinimide ester, and heterologous expression [Di Bernardo, S., and Yagi, T. (2001) FEBS Lett. 508, 385-388]. To further explore the near-neighbor relationship of the subunits, a zero-length cross-linker, 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC), and the Paracoccus membranes were used, and the cross-linked products were examined with antibodies specific to subunits Nqo1-11. The Nqo6 subunit was cross-linked to subunit Nqo9 (TYKY). In addition, a ternary product of Nqo3 (75k), Nqo6, and Nqo7 and binary products of Nqo3 and Nqo6 and of Nqo6 and Nqo7 were observed, but a binary product of Nqo3 and Nqo7 was not detected. The Nqo4 (49k) subunit was found to be associated with the Nqo7 subunit. Furthermore, Paracoccus subunits Nqo3, Nqo6, and Nqo7 were heterologously coexpressed in Escherichia coli, and EDC cross-linking experiments were carried out using the E. coli membranes expressing these three subunits. The results were the same as those obtained with Paracoccus membranes. On the basis of the data, subunit arrangements of NDH-1 were discussed.
Authors:
Mou-Chieh Kao; Akemi Matsuno-Yagi; Takao Yagi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  43     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-23     Completed Date:  2004-07-21     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3750-5     Citation Subset:  IM    
Affiliation:
Division of Biochemistry, Department of Molecular and Experimental Medicine, MEM-256, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
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MeSH Terms
Descriptor/Qualifier:
Cross-Linking Reagents / chemistry*
Escherichia coli / enzymology,  genetics
Ethyldimethylaminopropyl Carbodiimide / analogs & derivatives,  chemistry*
Iron-Sulfur Proteins / chemistry
Membrane Proteins / chemistry,  genetics
Paracoccus denitrificans / enzymology,  genetics
Protein Structure, Tertiary / genetics
Protein Subunits / chemistry*,  genetics
Proton-Translocating ATPases / chemistry
Quinone Reductases / chemistry*,  genetics
Recombinant Proteins / chemistry
Grant Support
ID/Acronym/Agency:
R01GM33712/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Cross-Linking Reagents; 0/Iron-Sulfur Proteins; 0/Membrane Proteins; 0/Protein Subunits; 0/Recombinant Proteins; 1892-57-5/Ethyldimethylaminopropyl Carbodiimide; 22572-40-3/1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide methiodide; EC 1.6.99.-/Quinone Reductases; EC 1.6.99.5/NADH dehydrogenase (quinone); EC 3.6.3.14/Proton-Translocating ATPases

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


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