ArticlePlant molecular biology1997
UDP-glucose:sterol glucosyltransferase: cloning and functional expression in Escherichia coli.
Article in Plant molecular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 91 citations in OpenAlex.
- A highly versatile fungal glucosyltransferase for specific production of quercetin-7-O-β-D-glucoside and quercetin-3-O-β-D-glucoside in different hosts.Applied microbiology and biotechnology · 2022Article
- Investigation ofInternational journal of molecular sciences · 2021Article
- Sterol Glucosyltransferases Tailor Polysaccharide Accumulation in Arabidopsis Seed Coat Epidermal Cells.Cells · 2021Article
- Steryl Glycosides in Fungal Pathogenesis: An Understudied Immunomodulatory Adjuvant.Journal of fungi (Basel, Switzerland) · 2020Review
- Inactivation of UDP-Glucose Sterol Glucosyltransferases EnhancesFrontiers in plant science · 2019Article
- Bioconversion of Corticosterone into Corticosterone-Glucoside by Glucosyltransferase.Molecules (Basel, Switzerland) · 2018Article
- Positioning of the SCRAMBLED receptor requires UDP-Glc:sterol glucosyltransferase 80B1 in Arabidopsis roots.Scientific reports · 2017Article
- TRANSPARENT TESTA 16 and 15 act through different mechanisms to control proanthocyanidin accumulation in Arabidopsis testa.Journal of experimental botany · 2017Article
- Tomato UDP-Glucose Sterol Glycosyltransferases: A Family of Developmental and Stress Regulated Genes that Encode Cytosolic and Membrane-Associated Forms of the Enzyme.Frontiers in plant science · 2017Article
- Plasma membrane lipids and their role in fungal virulence.Progress in lipid research · 2016Review
- Characterization of Arabidopsis sterol glycosyltransferase TTG15/UGT80B1 role during freeze and heat stress.Plant signaling & behavior · 2015Article
- Functional diversification of two UGT80 enzymes required for steryl glucoside synthesis in Arabidopsis.Journal of experimental botany · 2015Article
- Molecular cloning and biochemical characterization of a recombinant sterol 3-O-glucosyltransferase from Gymnema sylvestre R.Br. catalyzing biosynthesis of steryl glucosides.BioMed research international · 2014Article
- Article
- Sterol glycosyltransferases-identification of members of gene family and their role in stress in Withania somnifera.Molecular biology reports · 2012Article
- Article
- Deciphering the molecular functions of sterols in cellulose biosynthesis.Frontiers in plant science · 2012Article
- Quantification of sterol lipids in plants by quadrupole time-of-flight mass spectrometry.Journal of lipid research · 2011Article
- Triterpenoid biosynthesis and engineering in plants.Frontiers in plant science · 2011Article
- Mutations in UDP-Glucose:sterol glucosyltransferase in Arabidopsis cause transparent testa phenotype and suberization defect in seeds.Plant physiology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Steryl glucosides are characteristic lipids of plant membranes. The biosynthesis of these lipids is catalyzed by the membrane-bound UDP-glucose:sterol glucosyltransferase (EC 2.4.1.173). The purified enzyme (Warnecke and Heinz, Plant Physiol 105 (1994): 1067-1073) has been used for the cloning of a corresponding cDNA from oat (Avena sativa L.). Amino acid sequences derived from the amino terminus of the purified protein and from peptides of a trypsin digestion were used to construct oligonucleotide primers for polymerase chain reaction experiments. Screening of oat and Arabidopsis cDNA libraries with amplified labeled DNA fragments resulted in the isolation of sterol glucosyltransferase-specific cDNAs with insert lengths of ca. 2.3 kb for both plants. These cDNAs encode polypeptides of 608 (oat) and 637 (Arabidopsis) amino acid residues with molecular masses of 66 kDa and 69 kDa, respectively. The first amino acid of the purified oat protein corresponds to the amino acid 133 of the deduced polypeptide. The absence of these N-terminal amino acids reduces the molecular mass to 52 kDa, which is similar to the apparent molecular mass of 56 kDa determined for the purified protein. Different fragments of these cDNAs were expressed in Escherichia coli. Enzyme assays with homogenates of the transformed cells exhibited sterol glucosyltransferase activity.
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