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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1991-10-23
|
| pubmed:abstractText |
The frxC gene, one of the unidentified open reading frames present in liverwort chloroplast DNA, shows significant homology with the nifH genes coding for the Fe protein, a component of the nitrogenase complex (Ohyama et al., 1986, Nature 322: 572-574). A truncated form of the frxC gene was designed to be over-expressed in Escherichia coli and an antibody against this protein was prepared using the purified product as an antigen. This antibody reacted with a protein in the soluble fraction of liverwort chloroplasts, which had an apparent molecular weight of 31,000, as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, in good agreement with a putative molecular weight of 31,945 deduced from the DNA sequence of the frxC gene. In a competitive inhibition experiment, the antigenicity of this protein was indicated to be similar to that of the over-expressed protein in E. coli. Therefore, we concluded that the frxC gene was expressed in liverwort chloroplasts and that its product existed in a soluble form. The molecular weight of the frxC protein was approximately 67,000, as estimated by gel filtration chromatography, indicating that the frxC protein may exist as a dimer of two identical polypeptides analogous to the Fe protein of nitrogenase. The results obtained from affinity chromatography supported the possibility that the frxC protein, which possesses a ATP-binding sequence in its N-terminal region that is conserved among various other ATP-binding proteins, has the ability to bind ATP.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0167-4412
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
13
|
| pubmed:geneSymbol |
frxC,
nifH
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
551-61
|
| pubmed:dateRevised |
2009-8-13
|
| pubmed:meshHeading |
pubmed-meshheading:2491672-Adenosine Triphosphate,
pubmed-meshheading:2491672-Amino Acid Sequence,
pubmed-meshheading:2491672-Binding Sites,
pubmed-meshheading:2491672-Chloroplasts,
pubmed-meshheading:2491672-DNA,
pubmed-meshheading:2491672-Escherichia coli,
pubmed-meshheading:2491672-Gene Expression,
pubmed-meshheading:2491672-Genes, Bacterial,
pubmed-meshheading:2491672-Molecular Sequence Data,
pubmed-meshheading:2491672-Molecular Weight,
pubmed-meshheading:2491672-Nitrogen Fixation,
pubmed-meshheading:2491672-Plant Proteins,
pubmed-meshheading:2491672-Plants,
pubmed-meshheading:2491672-Plasmids
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Identification of a novel nifH-like (frxC) protein in chloroplasts of the liverwort Marchantia polymorpha.
|
| pubmed:affiliation |
Department of Biology, Faculty of Science, Osaka University, Japan.
|
| pubmed:publicationType |
Journal Article
|