Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-4-9
pubmed:databankReference
pubmed:abstractText
A cDNA (VUpur5) encoding phosphoribosyl aminoimidazole (AIR) synthetase, the fifth enzyme of the de novo purine biosynthesis pathway has been isolated from a cowpea nodule cDNA library. It encodes a 388 amino acid protein with a predicted molecular mass of 40.4 kDa. The deduced amino acid sequence has significant homology with AIR synthetase from other organisms. AIR synthetase is present in both mitochondria and plastids of cowpea nodules. A signal sequence encoded by the VUpur5 cDNA has properties associated with plastid transit sequences but there is no consensus cleavage site as would be expected for a plastid targeted protein. Although the signal sequence does not have the structural features of a mitochondrial targeted protein, it has a mitochondrial cleavage site motif (RX/XS) close to the predicted N-terminus of the mature protein. Southern analysis suggests that AIR synthetase is encoded by a single gene raising questions as to how the product of this gene is targeted to the two organelles. VUpur5 is expressed at much higher levels in nodules compared to other cowpea tissues and the gene is active before nitrogen fixation begins. These results suggest that products of nitrogen fixation do not play a role in the initial induction of gene expression. VUpur5 was expressed in Escherichia coli and the recombinant protein used to raise antibodies. These antibodies recognize two forms of AIR synthetase which differ in molecular size. Both forms are present in mitochondria, although the larger protein is more abundant. Only the smaller protein was detected in plastids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
811-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9520274-Amino Acid Sequence, pubmed-meshheading:9520274-Animals, pubmed-meshheading:9520274-Base Sequence, pubmed-meshheading:9520274-Carbon-Nitrogen Ligases, pubmed-meshheading:9520274-DNA, Complementary, pubmed-meshheading:9520274-DNA, Plant, pubmed-meshheading:9520274-Escherichia coli, pubmed-meshheading:9520274-Fabaceae, pubmed-meshheading:9520274-Gene Expression Regulation, Enzymologic, pubmed-meshheading:9520274-Humans, pubmed-meshheading:9520274-Mitochondria, pubmed-meshheading:9520274-Molecular Sequence Data, pubmed-meshheading:9520274-Organelles, pubmed-meshheading:9520274-Plants, Medicinal, pubmed-meshheading:9520274-Plastids, pubmed-meshheading:9520274-Recombinant Proteins, pubmed-meshheading:9520274-Sequence Alignment, pubmed-meshheading:9520274-Sequence Homology, Amino Acid
pubmed:year
1998
pubmed:articleTitle
AIR synthetase in cowpea nodules: a single gene product targeted to two organelles?
pubmed:affiliation
Department of Botany, The University of Western Australia, Nedlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't