rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1996-9-3
|
pubmed:databankReference |
|
pubmed:abstractText |
A cDNA with an open reading frame of 1929 bp (termed sir) was isolated from a lambda ZapII library of Arabidopsis thaliana leaf tissue. The polypeptide sequence deduced from the cDNA is homologous to the ferredoxin-dependent sulfite reductase (EC 1.8.7.1) from Synechococcus PCC7942 and distantly related to the hemoprotein subunit of Escherichia coli NADPH-dependent sulfite reductase (EC 1.8.1.2). A molecular mass of 71.98 kDa can be predicted for a ferredoxin sulfite reductase from A. thaliana. The polypeptide consists of 642 amino acids including a transit peptide of 66 residues (6.72 kDa) that is assumed to direct the protein into the plastid. For expression and enzymatic characterization of a putative A. thaliana ferredoxin sulfite reductase, the DNA of the transit peptide was deleted by a PCR method. The truncated cDNA clone was expressed as his-tag fusion protein. The modified gene product was enzymatically inactive but specific cross-reaction with polyclonal antibodies against ferredoxin sulfite reductase from Synechococcus is seen as confirmation of its identity as higher plant ferredoxin sulfite reductase.
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0006-3002
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
18
|
pubmed:volume |
1295
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
119-24
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8695637-Amino Acid Sequence,
pubmed-meshheading:8695637-Arabidopsis,
pubmed-meshheading:8695637-Arabidopsis Proteins,
pubmed-meshheading:8695637-Base Sequence,
pubmed-meshheading:8695637-Cyanobacteria,
pubmed-meshheading:8695637-DNA, Complementary,
pubmed-meshheading:8695637-Escherichia coli,
pubmed-meshheading:8695637-Molecular Sequence Data,
pubmed-meshheading:8695637-Molecular Weight,
pubmed-meshheading:8695637-Oxidoreductases Acting on Sulfur Group Donors,
pubmed-meshheading:8695637-Plastids,
pubmed-meshheading:8695637-Sequence Homology,
pubmed-meshheading:8695637-Sulfite Reductase (Ferredoxin),
pubmed-meshheading:8695637-Sulfite Reductase (NADPH)
|
pubmed:year |
1996
|
pubmed:articleTitle |
A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin:sulfite reductase.
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pubmed:affiliation |
Faculty of Biology, Ruhr University Bochum, Germany.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|