ArticlePlant physiology1996
Cloning of a cDNA encoding cytosolic acetoacetyl-coenzyme A thiolase from radish by functional expression in Saccharomyces cerevisiae.
Article in Plant physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 38 citations in OpenAlex.
- Digital Gene Expression Profiling to Explore Differentially Expressed Genes Associated with Terpenoid Biosynthesis during Fruit Development in Litsea cubeba.Molecules (Basel, Switzerland) · 2016Article
- Effect of nitrogen and temperature on the transcription of an ACAT gene in Isochrysis galbana.Molecular biology reports · 2014Article
- Expression of 3-hydroxy-3-methylglutaryl-CoA reductase, p-hydroxybenzoate-m-geranyltransferase and genes of phenylpropanoid pathway exhibits positive correlation with shikonins content in arnebia [Arnebia euchroma (Royle) Johnston].BMC molecular biology · 2010Article
- Phylogenetic analysis of eukaryotic thiolases suggests multiple proteobacterial origins.Journal of molecular evolution · 2005Article
- Genome organization in Arabidopsis thaliana: a survey for genes involved in isoprenoid and chlorophyll metabolism.Plant molecular biology · 2003Article
- Farnesol-induced cell death and stimulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity in tobacco cv bright yellow-2 cells.Plant physiology · 2000Article
- Acetyl Coenzyme A Acetyltransferase of Rhizobium sp. (Cicer) Strain CC 1192.Applied and environmental microbiology · 1997Article
- The PmRDUF1-PmMYB30-PmLAS Regulatory Module Is Involved in Terpenoid Biosynthesis of Pinus massoniana.Physiologia plantarumArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A cDNA coding for radish (Raphanus sativus L.) acetoacetyl-coenzyme A thiolase (AACT) was cloned by complementation of the erg10 mutation affecting AACT in yeast (Saccharomyces cerevisiae). The longest reading frame encodes a protein of 406 amino acids with a predicted relative molecular weight of 42,032, with significant similarities to eukaryotic and prokaryotic thiolases. There is no evidence for the presence of a leader peptide characteristic, e.g. of glyoxysomal thiolase. Yeast transformants expressing the radish AACT gene placed under the control of the GAL1 promoter exhibited a 10-fold higher enzyme activity than a wild-type yeast strain after induction by galactose. This enzyme activity is exclusively localized in the soluble fraction but not in membranes. These data indicate that we have cloned a gene encoding cytoplasmic (biosynthetic) AACT. Genomic DNA gel blot analysis suggests the presence of a single AACT gene, which is expressed in all parts of the seedling. Expression in cotyledons appears to be light-stimulated. We present preliminary evidence that a smaller transcript represents an antisense species being read from the same gene.
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