ArticlePlant molecular biology2008
Arabidopsis thaliana contains a single gene encoding squalene synthase.
Article in Plant molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 79 citations in OpenAlex.
- The potential of metabolic engineering for sustainable phytosterol production.Advanced biotechnology · 2026Review
- Genome-Wide Identification and Expression Analysis ofBiology · 2026Article
- Discovery of an SQS-PSY Domain-Containing Protein inInternational journal of molecular sciences · 2025Article
- Are there conserved biosynthetic genes in lichens? Genome-wide assessment of terpene biosynthetic genes suggests ubiquitous distribution of the squalene synthase cluster.BMC genomics · 2024Article
- Integrating QTL mapping and transcriptomics to decipher the genetic architecture of sterol metabolism inHorticulture research · 2024Article
- Reclassification of Botryococcus braunii chemical races into separate species based on a comparative genomics analysis.PloS one · 2024Article
- Functional Characterization of Four Olive Squalene Synthases with Respect to the Squalene Content of the Virgin Olive Oil.Journal of agricultural and food chemistry · 2023Article
- Arabidopsis 3β-Hydroxysteroid Dehydrogenases/C4-Decarboxylases Are Essential for the Pollen and Embryonic Development.International journal of molecular sciences · 2023Article
- Heterologous expression of Chlorophytum borivilianum Squalene epoxidase in tobacco modulates stigmasterol production and alters vegetative and reproductive growth.Plant cell reports · 2023Article
- The Identification ofMolecules (Basel, Switzerland) · 2023Article
- Natural variation and underlying genetic loci of γ-oryzanol in Asian cultivated rice seeds.The plant genome · 2022Article
- Phytosterol metabolism in plant positive-strand RNA virus replication.Plant cell reports · 2022Review
- The subcellular localization of two isopentenyl diphosphate isomerases in rice suggests a role for the endoplasmic reticulum in isoprenoid biosynthesis.Plant cell reports · 2020Article
- Molecular Cloning and Functional Identification of a Squalene Synthase Encoding Gene from Alfalfa (International journal of molecular sciences · 2019Article
- Metabolic Innovations Underpinning the Origin and Diversification of the Diatom Chloroplast.Biomolecules · 2019Review
- Positive Selection of Squalene Synthase in Cucurbitaceae Plants.International journal of genomics · 2019Article
- Squalene synthase cloning and functional identification in wintersweet plant (Chimonanthus zhejiangensis).Botanical studies · 2018Article
- Functional characterization of squalene synthase and squalene epoxidase inPlant direct · 2018Article
- Cloning, Expression Analysis and Functional Characterization of Squalene Synthase (SQS) from Tripterygium wilfordii.Molecules (Basel, Switzerland) · 2018Article
- Identification and cytochemical immunolocalization of acetyl-CoA acetyltransferase involved in the terpenoid mevalonate pathway in Euphorbia helioscopia laticifers.Botanical studies · 2017Article
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7 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Squalene synthase (SQS) catalyzes the condensation of two molecules of farnesyl diphosphate (FPP) to produce squalene (SQ), the first committed precursor for sterol, brassinosteroid, and triterpene biosynthesis. Arabidopsis thaliana contains two SQS-annotated genomic sequences, At4g34640 (SQS1) and At4g34650 (SQS2), organized in a tandem array. Here we report that the SQS1 gene is widely expressed in all tissues throughout plant development, whereas SQS2 is primarily expressed in the vascular tissue of leaf and cotyledon petioles, and the hypocotyl of seedlings. Neither the complete A. thaliana SQS2 protein nor the chimeric SQS resulting from the replacement of the 69 C-terminal residues of SQS2 by the 111 C-terminal residues of the Schizosaccharomyces pombe SQS were able to confer ergosterol prototrophy to a Saccharomyces cerevisiae erg9 mutant strain lacking SQS activity. A soluble form of SQS2 expressed in Escherichia coli and purified was unable to synthesize SQ from FPP in the presence of NADPH and either Mg2+ or Mn2+. These results demonstrated that SQS2 has no SQS activity, so that SQS1 is the only functional SQS in A. thaliana. Mutational studies revealed that the lack of SQS activity of SQS2 cannot be exclusively attributed to the presence of an unusual Ser replacing the highly conserved Phe at position 287. Expression of green fluorescent protein (GFP)-tagged versions of SQS1 in onion epidermal cells demonstrated that SQS1 is targeted to the endoplasmic reticulum (ER) membrane and that this location is exclusively dependent on the presence of the SQS1 C-terminal hydrophobic trans-membrane domain.
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