Source:http://linkedlifedata.com/resource/pubmed/id/10608658
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2000-1-10
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| pubmed:databankReference | |
| pubmed:abstractText |
Recently, we purified to homogeneity and characterized a low-molecular-weight calcium-dependent phospholipase A2 (PLA2) from developing elm seed endosperm. This represented the first purified and characterized PLA2 from a plant tissue. The full sequences of two distinct but homologous rice (Oryza sativa) cDNAs are given here. These encode mature proteins of 1 19 amino acids (PLA2-I, preceded by a 19 amino acid signal peptide) and 128 amino acids (PLA2-II. preceded by a 25 amino acid signal peptide), and were derived from four expressed sequence tag (EST) clones. Both proteins were homologous to the N-terminal amino acid sequence of the elm PLA2. They contained twelve conserved cysteine residues and sequences that are likely to represent the Ca(2+)-binding loop and active-site motif, which are characteristic of animal secretory PLA2s. A soluble PLA2s activity was purified 145 000-fold from green rice shoots. This had the same biochemical characteristics as the elm and animal secretory PLA2s. The purified rice PLA2 consisted of two proteins, with a molecular weight of 12 440 and 12 920, that had identical N-terminal amino acid sequences. This sequence was different from but homologous to the PLA2-I and PLA2-II sequences. Taken together, the results suggest that at least three different low-molecular-weight PLA2s are expressed in green rice shoots. Southern blot analysis suggested that multiple copies of such genes are likely to occur in the rice and in other plant genomes.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0167-4412
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
41
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
481-90
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10608658-Amino Acid Sequence,
pubmed-meshheading:10608658-Animals,
pubmed-meshheading:10608658-Blotting, Southern,
pubmed-meshheading:10608658-DNA, Complementary,
pubmed-meshheading:10608658-DNA, Plant,
pubmed-meshheading:10608658-Expressed Sequence Tags,
pubmed-meshheading:10608658-Isoenzymes,
pubmed-meshheading:10608658-Molecular Sequence Data,
pubmed-meshheading:10608658-Molecular Weight,
pubmed-meshheading:10608658-Oryza sativa,
pubmed-meshheading:10608658-Phospholipases A,
pubmed-meshheading:10608658-Phospholipases A2,
pubmed-meshheading:10608658-Sequence Alignment,
pubmed-meshheading:10608658-Sequence Analysis, DNA,
pubmed-meshheading:10608658-Sequence Analysis, Protein,
pubmed-meshheading:10608658-Sequence Homology, Amino Acid,
pubmed-meshheading:10608658-Substrate Specificity,
pubmed-meshheading:10608658-Trees
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| pubmed:year |
1999
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| pubmed:articleTitle |
Plant low-molecular-weight phospholipase A2S (PLA2s) are structurally related to the animal secretory PLA2s and are present as a family of isoforms in rice (Oryza sativa).
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| pubmed:affiliation |
Department of Plant Biology, Swedish University of Agricultural Sciences, Uppsala.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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