ArticleProceedings of the National Academy of Sciences of the United States of America1999
Protein prenylation in spinach chloroplasts.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Chloroplastic protein prenylation: an internal or external affair? Reconciling biochemical data through a new hypothesis.Frontiers in plant science · 2026Article
- Protein Prenylation Makeovers in Plants: Insights into Substrate Diversification.International journal of molecular sciences · 2025Review
- TkSRPP3/4 interactors TkGGR1 and TkLIL3 link plastid-like organelles with isoprenoid metabolism in Taraxacum koksaghyz latex.Plant cell reports · 2025Article
- PEDF Protects Endothelial Barrier Integrity during Acute Myocardial Infarction via 67LR.International journal of molecular sciences · 2023Article
- Potentiating Vγ9Vδ2 T cell proliferation and assessing their cytotoxicity towards adherent cancer cells at the single cell level.Biology open · 2022Article
- Isoprenoid alcohols utilization by malaria parasites.Frontiers in chemistry · 2022Article
- The Plastoglobule-Localized Metallopeptidase PGM48 Is a Positive Regulator of Senescence in Arabidopsis thaliana.The Plant cell · 2016Article
- Multi-Substrate Terpene Synthases: Their Occurrence and Physiological Significance.Frontiers in plant science · 2016Review
- Posttranslational Protein Modifications in Plant Metabolism.Plant physiology · 2015Article
- A bifunctional geranyl and geranylgeranyl diphosphate synthase is involved in terpene oleoresin formation in Picea abies.Plant physiology · 2010Article
- Article
- Genome organization in Arabidopsis thaliana: a survey for genes involved in isoprenoid and chlorophyll metabolism.Plant molecular biology · 2003Article
- Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein prenylation in plants was studied by in vivo metabolic (3)H-mevalonate labeling in combination with a range of protein synthesis inhibitors. In spinach cotyledons, this posttranslational protein modification was found to be divided into two categories, one representing the conventional prenylation involving farnesyl and geranylgeranyl groups bound to cysteine residues via thioether linkages. This category revealed a similar pattern of prenylated proteins to that observed in mammalian cells and depends on nuclear gene expression. The other category was shown to represent a type of prenylation confined to chloroplasts. It depends on plastid gene expression and does not involve a thioether bond. The modifying isoprenoid could be released from the chloroplastic polypeptides by alkaline treatment and was identified as phytol upon GC-MS analysis. The phytol could readily be derived from all-trans-[(3)H]farnesol, which, like all-trans-[(3)H]geranylgeraniol, was taken up by the cotyledons, resulting in incorporation of radiolabel into proteins.
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