Linked Life Data

11247608

Source:http://linkedlifedata.com/resource/pubmed/id/11247608

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-3-14
pubmed:databankReference
pubmed:abstractText
A vast array of triterpenes are found in living organisms in addition to lanosterol and cycloartenol, which are involved in sterol biosynthesis in non-photosynthetic and photosynthetic eukaryotes respectively. The chemical structure of these triterpenes is determined by a single step catalysed by 2,3-oxidosqualene-triterpene cyclases. The present study describes cloning and functional expression in yeast of several OS-triterpene cyclases. Three Arabidopsis thaliana cDNAs encoding proteins (ATLUP1, ATLUP2, ATPEN1) 57%, 58% and 49% identical to cycloartenol synthase from the same plant were isolated. Expression of these cDNAs in yeast showed that the recombinant proteins catalyse the synthesis of various pentacyclic triterpenes. Whereas ATLUP1 is essentially involved in the synthesis of lupeol, ATLUP2 catalyses the production of lupeol, beta- and alpha-amyrin (in a 15:55:30 ratio). ATLUP2 is therefore a typical multifunctional enzyme. Under the same conditions, ATPEN1 did not lead to any product. Systematic sequencing of the Arabidopsis genome has led to genomic sequences encoding proteins identical to the above triterpene synthases. ATLUPI and ATLUP2 are representative of a small subfamily (A) of at least five genes, whereas ATPEN1 is representative of a subfamily (B) of at least seven genes. The number of introns is characteristic of each subfamily. Whereas genes of family A possess 17 exons and 16 introns, genes of the subfamily B contain 14 exons and 13 introns. The size of each exon is remarkably conserved within each subfamily whereas that of each intron appears to be highly variable. Organization of the genes, sequences and functions of the deduced proteins are discussed in evolutionary terms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-92
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:11247608-Amino Acid Sequence, pubmed-meshheading:11247608-Arabidopsis, pubmed-meshheading:11247608-Cloning, Molecular, pubmed-meshheading:11247608-DNA, Complementary, pubmed-meshheading:11247608-DNA, Recombinant, pubmed-meshheading:11247608-Gene Expression Regulation, Enzymologic, pubmed-meshheading:11247608-Genes, Plant, pubmed-meshheading:11247608-Intramolecular Transferases, pubmed-meshheading:11247608-Molecular Sequence Data, pubmed-meshheading:11247608-Oleanolic Acid, pubmed-meshheading:11247608-Pentacyclic Triterpenes, pubmed-meshheading:11247608-Phylogeny, pubmed-meshheading:11247608-Plasmids, pubmed-meshheading:11247608-Saccharomyces cerevisiae, pubmed-meshheading:11247608-Sequence Alignment, pubmed-meshheading:11247608-Sequence Analysis, DNA, pubmed-meshheading:11247608-Sequence Homology, Amino Acid, pubmed-meshheading:11247608-Triterpenes
pubmed:year
2001
pubmed:articleTitle
Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana.
pubmed:affiliation
Institut de Biologie Moléculaire des Plantes du CNRS, Institut de Botanique, Strasbourg, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't