Linked Life Data

15102833

Source:http://linkedlifedata.com/resource/pubmed/id/15102833

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
2004-6-28
pubmed:abstractText
Cyanobacteria contain several genes, annotated ndh, whose products show sequence similarities to subunits found in complex I (NADH:ubiquinone oxidoreductase) of eubacteria and mitochondria. However, it is still unclear whether the cyanobacterial ndh gene products actually form a single large protein complex or exist as smaller independent complexes. To address this, we have constructed a strain of Synechocystis sp. PCC 6803 in which the C terminus of the NdhJ subunit was fused to an His(6) tag to aid isolation. Three major NdhJ-containing complexes were resolved by blue native polyacrylamide gel electrophoresis, with approximate apparent molecular masses of 460, 330, and 110 kDa. N-terminal sequencing and mass spectrometry revealed that the 460-kDa complex contained ten annotated ndh gene products. Detergent-induced fragmentation experiments indicated that the 460-kDa complex was composed of hydrophobic (150 kDa) and hydrophilic (110-130 kDa) modules similar to that found in the minimal form of complex I found in Escherichia coli, except that the electron input module was not conserved. The difference in size between the 460- and 330-kDa complexes is attributed to differences in the stoichiometry of the hydrophilic and hydrophobic modules in the complex, either 2:1 or 1:1, respectively. We have also detected the presence of two new Ndh subunits (slr1623 and sll1262) that are unrelated to subunits in the eubacterial complex I but which have homologues in the closely related chloroplast Ndh complex of maize (Funk, E., Schäfer, E., and Steinmüller, K. (1999) J. Plant Physiol. 154, 16-23). The presence of these additional subunits might reflect the use by the NDH-1 and Ndh complexes of a different, so far unidentified, electron input module.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
28165-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15102833-Amino Acid Sequence, pubmed-meshheading:15102833-Cell Nucleus, pubmed-meshheading:15102833-Chloroplasts, pubmed-meshheading:15102833-Chromatography, Liquid, pubmed-meshheading:15102833-Computational Biology, pubmed-meshheading:15102833-Cyanobacteria, pubmed-meshheading:15102833-Detergents, pubmed-meshheading:15102833-Electron Transport Complex I, pubmed-meshheading:15102833-Electrons, pubmed-meshheading:15102833-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15102833-Escherichia coli, pubmed-meshheading:15102833-Immunoblotting, pubmed-meshheading:15102833-Mass Spectrometry, pubmed-meshheading:15102833-Molecular Sequence Data, pubmed-meshheading:15102833-NADP, pubmed-meshheading:15102833-NADPH Dehydrogenase, pubmed-meshheading:15102833-Protein Structure, Tertiary, pubmed-meshheading:15102833-Quinone Reductases, pubmed-meshheading:15102833-Sequence Homology, Amino Acid, pubmed-meshheading:15102833-Software
pubmed:year
2004
pubmed:articleTitle
Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803: identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex.
pubmed:affiliation
Department of Biological Sciences, Wolfson Laboratories, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't