ArticlePlant physiology2001
Efficient prenylation by a plant geranylgeranyltransferase-I requires a functional CaaL box motif and a proximal polybasic domain.
Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 61 citations in OpenAlex.
- Protein Prenylation Makeovers in Plants: Insights into Substrate Diversification.International journal of molecular sciences · 2025Review
- Barley resistance and susceptibility to fungal cell entry involve the interplay of ROP signaling with phosphatidylinositol-monophosphates.The Plant journal : for cell and molecular biology · 2025Article
- Protein Prenylation in Plants: Mechanisms and Functional Implications.Plants (Basel, Switzerland) · 2025Review
- Stimulation of adventitious root formation by the oligosaccharin OSRG at the transcriptome level.Plant signaling & behavior · 2020Article
- Probing the function of protein farnesyltransferase in Tripterygium wilfordii.Plant cell reports · 2019Article
- The role of lipid post-translational modification in plant developmental processes.Frontiers in plant science · 2014Review
- An effective system for detecting protein-protein interaction based on in vivo cleavage by PPV NIa protease.Protein & cell · 2012Article
- ROP GTPases act with the receptor-like protein PAN1 to polarize asymmetric cell division in maize.The Plant cell · 2011Article
- Differential effects of prenylation and s-acylation on type I and II ROPS membrane interaction and function.Plant physiology · 2011Article
- Characterization, sub-cellular localization and expression profiling of the isoprenylcysteine methylesterase gene family in Arabidopsis thaliana.BMC plant biology · 2010Article
- The CaaX specificities of Arabidopsis protein prenyltransferases explain era1 and ggb phenotypes.BMC plant biology · 2010Article
- Farnesylcysteine lyase is involved in negative regulation of abscisic acid signaling in Arabidopsis.Molecular plant · 2010Article
- Shoot-specific down-regulation of protein farnesyltransferase (alpha-subunit) for yield protection against drought in canola.Molecular plant · 2009Article
- Proteins prenylated by type I protein geranylgeranyltransferase act positively on the jasmonate signalling pathway triggering the biosynthesis of monoterpene indole alkaloids in Catharanthus roseus.Plant cell reports · 2009Article
- The plastidial 2-C-methyl-D-erythritol 4-phosphate pathway provides the isoprenyl moiety for protein geranylgeranylation in tobacco BY-2 cells.The Plant cell · 2009Article
- Heterelogous expression of plant genes.International journal of plant genomics · 2009Article
- Isoprenylcysteine methylation and demethylation regulate abscisic acid signaling in Arabidopsis.The Plant cell · 2008Article
- Functional analysis of Arabidopsis postprenylation CaaX processing enzymes and their function in subcellular protein targeting.Plant physiology · 2008Article
- Regulation of membrane trafficking, cytoskeleton dynamics, and cell polarity by ROP/RAC GTPases.Plant physiology · 2008Article
- Ggamma1 + Ggamma2 not equal to Gbeta: heterotrimeric G protein Ggamma-deficient mutants do not recapitulate all phenotypes of Gbeta-deficient mutants.Plant physiology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Geranylgeranyltransferase-I (GGT-I) is a heterodimeric enzyme that shares a common alpha-subunit with farnesyltransferase (FTase) and has a distinct beta-subunit. GGT-I preferentially modifies proteins, which terminate in a CaaL box sequence motif. Cloning of Arabidopsis GGT-I beta-subunit (AtGGT-IB) was achieved by a yeast (Saccharomyces cerevisiae) two-hybrid screen, using the tomato (Lycopersicon esculentum) FTase alpha-subunit (FTA) as bait. Sequence and structure analysis revealed that the core active site of GGT-I and FTase are very similar. AtGGT-IA/FTA and AtGGT-IB were co-expressed in baculovirus-infected insect cells to obtain recombinant protein that was used for biochemical and molecular analysis. The recombinant AtGGT-I prenylated efficiently CaaL box fusion proteins in which the a(2) position was occupied by an aliphatic residue, whereas charged or polar residues at the same position greatly reduced the efficiency of prenylation. A polybasic domain proximal to the CaaL box motif induced a 5-fold increase in the maximal reaction rate, and increased the affinity of the enzyme to the protein substrate by an order of magnitude. GGT-I retained high activity in a temperature range between 24 degrees C and 42 degrees C, and showed increased activity rate at relatively basic pH values of 7.9 and 8.5. Reverse transcriptase-polymerase chain reaction, protein immuno-blots, and transient expression assays of green fluorescent protein fusion proteins show that GGT-IB is ubiquitously expressed in a number of tissues, and that expression levels and protein activity were not changed in mutant plants lacking FTase beta-subunit.
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