The N-terminal Domain of Tomato 3-Hydroxy-3-methylglutaryl-CoA Reductases
Open accessAbstract
The enzyme 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the conversion of 3-hydroxy-3-methylglutaryl-CoA to mevalonic acid, considered the rate-limiting step in isoprenoid biosynthesis. In plants, isoprenoid compounds play important roles in mediating plant growth and development, electron transport, photosynthesis, and disease resistance. Sequence comparisons of plant HMGR proteins with those from yeast and mammalian systems reveal high levels of sequence identity within the catalytic domain but significant divergence in the membrane domain. Mammalian HMGRs are integral membrane proteins of the endoplasmic reticulum with eight membrane-spanning regions. In contrast, the membrane domain of plant HMGRs is predicted to contain only one to two transmembrane spans. We have isolated and sequenced a clone (pCD4) encoding exon 1 of tomato hmg1. The membrane domain structures of two differentially regulated tomato HMGR isoforms, HMG1 and HMG2, were analyzed using in vitro transcription and translation systems. Microsomal membrane insertion of the tomato HMGRs is co-translational and does not involve cleavage of an N-terminal targeting peptide. HMGR membrane topography was established by protease protection studies of the HMG1 membrane domain and an analogous region of HMG2 engineered to contain a c-myc epitope tag. The data indicate that both tomato HMGRs span the membrane two times with both the C and N termini located in the cytosol. Lumenal localization of the short peptide predicted to lie within the endoplasmic reticulum was further confirmed by in vitro glycosylation of an asparagine-linked glycosylation site present in HMG2.
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The mevalonic acid (MVA) pathway operates in the cytosol, the endoplasmic reticulum, and peroxisomes.
“The mevalonic acid (MVA) pathway operates in the cytosol (early steps), the endoplasmic reticulum (3-hydroxy-3-methylglutaryl-CoA reductase) and peroxisomes (late steps)”
From Metabolic engineering of plant monoterpenes, sesquiterpenes and diterpenes—current status and future opportunities (2013) · cites this paper as Denbow et al., 1996
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- Authors
- Denbow, C. J., Lång, S., & Cramer, C. L.
- Affiliations
- Virginia Tech (US)
- Corresponding author
- Cramer, Carole L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-04
- Volume
- 271
- Issue
- 16
- Pages
- 9710-9715
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1510518889
- Cited by
- 52
- References
- 46
- Citations by year
- 2024: 3 · 2022: 2 · 2021: 1 · 2018: 1 · 2017: 3 · 2015: 1 · 2014: 2 · 2013: 4 · 2012: 2
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Agriculture
- National Institutes of Health (5r29gm039549-05)
- National Institute of General Medical Sciences (R29-GM39549)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- 3-hydroxy-3-methylglutaryl-CoA reductase, HMG1, HMG2, N-terminal domain, membrane domains, transmembrane topology, isoprenoid biosynthesis, mevalonate, endoplasmic reticulum membrane insertion, co-translational insertion, asparagine-linked glycosylation, protein isoforms, plant sterol biosynthesis
- MeSH terms
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Glycosylation, Hydroxymethylglutaryl CoA Reductases, Intracellular Membranes, Microsomes, Molecular Sequence Data, Plants, Protein Processing, Post-Translational, Recombinant Proteins, Species Specificity, Protein Biosynthesis, Polymerase Chain Reaction, Sequence Homology, Amino Acid, Protein Structure, Secondary, DNA Primers, DNA, Complementary, Solanum lycopersicum
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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