Linked Life Data

16926158

Source:http://linkedlifedata.com/resource/pubmed/id/16926158

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
43
pubmed:dateCreated
2006-10-23
pubmed:databankReference
pubmed:abstractText
Graminaceous plants have evolved a unique mechanism to acquire iron through the secretion of a family of small molecules, called mugineic acid family phytosiderophores (MAs). All MAs are synthesized from l-Met, sharing the same pathway from l-Met to 2'-deoxymugineic acid (DMA). DMA is synthesized through the reduction of a 3''-keto intermediate by deoxymugineic acid synthase (DMAS). We have isolated DMAS genes from rice (OsDMAS1), barley (HvDMAS1), wheat (TaD-MAS1), and maize (ZmDMAS1). Their nucleotide sequences indicate that OsDMAS1 encodes a predicted polypeptide of 318 amino acids, whereas the other three orthologs all encode predicted polypeptides of 314 amino acids and are highly homologous (82-97.5%) to each other. The DMAS proteins belong to the aldo-keto reductase superfamily 4 (AKR4) but do not fall within the existing subfamilies of AKR4 and appear to constitute a new subfamily within the AKR4 group. All of the proteins showed DMA synthesis activity in vitro. Their enzymatic activities were highest at pH 8-9, consistent with the hypothesis that DMA is synthesized in subcellular vesicles. Northern blot analysis revealed that the expression of each of the above DMAS genes is up-regulated under iron-deficient conditions in root tissue, and that of the genes OsDMAS1 and TaDMAS1 is up-regulated in shoot tissue. OsDMAS1 promoter-GUS analysis in iron-sufficient roots showed that its expression is restricted to cells participating in long distance transport and that it is highly up-regulated in the entire root under iron-deficient conditions. In shoot tissue, OsDMAS1 promoter drove expression in vascular bundles specifically under iron-deficient conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32395-402
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:16926158-Amino Acid Sequence, pubmed-meshheading:16926158-Azetidinecarboxylic Acid, pubmed-meshheading:16926158-Cloning, Molecular, pubmed-meshheading:16926158-Genes, Plant, pubmed-meshheading:16926158-Hordeum, pubmed-meshheading:16926158-Hydrogen-Ion Concentration, pubmed-meshheading:16926158-Immunohistochemistry, pubmed-meshheading:16926158-Iron, pubmed-meshheading:16926158-Mixed Function Oxygenases, pubmed-meshheading:16926158-Molecular Sequence Data, pubmed-meshheading:16926158-Oryza sativa, pubmed-meshheading:16926158-Phylogeny, pubmed-meshheading:16926158-Plant Roots, pubmed-meshheading:16926158-Plants, Genetically Modified, pubmed-meshheading:16926158-Plasmids, pubmed-meshheading:16926158-Promoter Regions, Genetic, pubmed-meshheading:16926158-Recombinant Proteins, pubmed-meshheading:16926158-Sequence Homology, Amino Acid, pubmed-meshheading:16926158-Siderophores, pubmed-meshheading:16926158-Triticum, pubmed-meshheading:16926158-Zea mays
pubmed:year
2006
pubmed:articleTitle
Cloning and characterization of deoxymugineic acid synthase genes from graminaceous plants.
pubmed:affiliation
Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657.
pubmed:publicationType
Journal Article, Comparative Study