Protein Farnesyltransferase in Plants (Molecular Cloning and Expression of a Homolog of the [beta] Subunit from the Garden Pea)

Yang, Zhenbiao; Cramer, Carole L.; Watson, John C.

doi:10.1104/pp.101.2.667

Cited by 45 publications

(33 citation statements)

References 51 publications

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“…Protein prenylation in plants has recently been reported (Randall et al, 1993;Zhu et al, 1993). A farnesyl transferase subunit has been cloned from plants, and its expression pattern suggests that farnesyl transferase may have acritical role in regulating plant cell growth and division (Yang et al, 1993). The observation that the HMGP gene is expressed in the Arabidopsis T87 cell suspension culture (data not shown) further reinforces the proposed key role of HMGR2 in cell division.…”

Section: Discussionsupporting

confidence: 60%

Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues.

et al. 1995

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M o n t s e r r a t Enjuto,' Victoria Lumbreras, Carles Marín, a n d A l b e r t B o r o n a t 2 Unitat de Bioquímica i Biologia Molecular A, Departament de Bioquímica i Fisiologia, Facultat de Química, Universitat de Barcelona, 08028 Barcelona, SpainThe synthesis of mevalonate, which is considered the first rate-limiting step in isoprenoid biosynthesis, is catalyzed by the enzyme 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR; EC 1.1.1.34). In Arabidopsis, HMGR is encoded by two differentially expressed genes (HMG1 and HMGP). The transcriptional activity of the HMGP gene was studied after fusing different regions of its 5' flanking region to the P-glucuronidase (GUS) reporter gene and transforming the resulting constructs into tobacco plants. The spatial and temporal expression directed by the HMGP promoter in the transgenic plants is consistent with the expression pattern previously established by RNA analysis using an HMGBspecific probe. HMGP expression is restricted to meristematic (root tip and shoot apex) and floral (secretory zone of the stigma, mature pollen grains, gynoecium vascular tissue, and fertilized ovules) tissues. Deletion analysis of the HMGP 5'flanking region was conducted in transgenic plants and transfected protoplasts. The region containing nucleotides -857 to +64 of the HMGP gene was sufficient to confer high levels of expression in both floral and meristematic tissues, although deletion to nucleotide -503 resulted in almost complete loss of expression. Sequences contained within the 5' transcribed, untranslated region are also important for gene expression. The biological significance of the restricted pattern of expression of HMGP is also discussed.

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Section: Discussionsupporting

confidence: 60%

Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues.

et al. 1995

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“…A third enzyme, protein geranylgeranyltransferase type II (PGGT II), also called RAB geranylgeranyltransferase (RAB GGT), catalyzes the geranylgeranylation of RAB proteins bound to the RAB ESCORT PROTEIN. All three enzymes have been found in protozoans, metazoans, fungi, and plants, including pea (Pisum sativum) (Yang et al, 1993;Qian et al, 1996), tomato (Solanum lycopersicum) Yalovsky et al, 1996), and Arabidopsis thaliana (Cutler et al, 1996;Pei et al, 1998;Caldelari et al, 2001;Running et al, 2004;Johnson et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Isoprenylcysteine Methylation and Demethylation Regulate Abscisic Acid Signaling inArabidopsis

et al. 2008

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Isoprenylated proteins bear an isoprenylcysteine methyl ester at the C terminus. Although isoprenylated proteins have been implicated in meristem development and negative regulation of abscisic acid (ABA) signaling, the functional role of the terminal methyl group has not been described. Here, we show that transgenic Arabidopsis thaliana plants overproducing isoprenylcysteine methyltransferase (ICMT) exhibit ABA insensitivity in stomatal closure and seed germination assays, establishing ICMT as a negative regulator of ABA signaling. By contrast, transgenic plants overproducing isoprenylcysteine methylesterase (ICME) exhibit ABA hypersensitivity in stomatal closure and seed germination assays. Thus, ICME is a positive regulator of ABA signaling. To test the hypothesis that ABA signaling is under feedback regulation at the level of isoprenylcysteine methylation, we examined the effect of ABA on ICMT and ICME gene expression. Interestingly, ABA induces ICME gene expression, establishing a positive feedback loop whereby ABA promotes ABA responsiveness of plant cells via induction of ICME expression, which presumably results in the demethylation and inactivation of isoprenylated negative regulators of ABA signaling. These results suggest strategies for metabolic engineering of crop species for drought tolerance by targeted alterations in isoprenylcysteine methylation.

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“…The farnesylation of ANJ1 is crucial for membrane binding and function at high temperatures (56). A gene encoding a putative FTase ␤ subunit has been cloned from pea (53), but evidence that this gene encodes a farnesyltransferase subunit was based solely on homology. Recently, the plant FTase was shown to be biochemically similar to the mammalian FTase and distinct from GGTase-I activity (47).…”

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confidence: 99%

Plant Farnesyltransferase Can Restore Yeast Ras Signaling and Mating

Yalovsky

Trueblood

Callan

et al. 1997

Molecular and Cellular Biology

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Farnesyltransferase (FTase) is a heterodimeric enzyme that modifies a group of proteins, including Ras, in mammals and yeasts. Plant FTase ␣ and ␤ subunits were cloned from tomato and expressed in the yeast Saccharomyces cerevisiae to assess their functional conservation in farnesylating Ras and a-factor proteins, which are important for cell growth and mating. The tomato FTase ␤ subunit (LeFTB) alone was unable to complement the growth defect of ram1⌬ mutant yeast strains in which the chromosomal FTase ␤ subunit gene was deleted, but coexpression of LeFTB with the plant ␣ subunit gene (LeFTA) restored normal growth, Ras membrane association, and mating. LeFTB contains a novel 66-amino-acid sequence domain whose deletion reduces the efficiency of tomato FTase to restore normal growth to yeast ram1⌬ strains. Coexpression of LeFTA and LeFTB in either yeast or insect cells yielded a functional enzyme that correctly farnesylated CaaX-motifcontaining peptides. Despite their low degree of sequence homology, yeast and plant FTases shared similar in vivo and in vitro substrate specificities, demonstrating that this enzymatic modification of proteins with intermediates from the isoprenoid biosynthesis pathway is conserved in evolutionarily divergent eukaryotes.Modification of various proteins by the C 15 isoprene farnesyl or the C 20 isoprene geranylgeranyl groups facilitates their adherence to membranes and, for some proteins that have been studied in detail, is also required for their function (34,44,54). Protein prenylation was discovered almost 2 decades ago as a modification of peptide mating pheromones produced by fungi (28,43). During the last 8 years, a growing number of proteins have been discovered that are prenylated. Interestingly, many of these proteins play key roles in the regulation of cell division, cell growth, and signal transduction processes. These proteins include normal and oncogenic forms of Ras, the yeast a-factor mating pheromone, certain ␥ subunits of heterotrimeric G proteins, proteins in the vertebrate visual system, hepatitis delta virus large antigen, and type I inositol triphosphate 5Ј-phosphatase (1,2,11,16,18,23,25,26,30,36,45,52).All known farnesylated proteins have a common C-terminal sequence motif known as the CaaX box (C, cysteine; a, usually an aliphatic amino acid; X, any amino acid). Yeast and mammalian protein farnesyltransferases (FTases) attach the farnesyl group from farnesyl pyrophosphate via a thioether linkage to the cysteines of CaaX sequences in which X is serine, methionine, cysteine, alanine, or glutamine (44). In most cases, farnesylation is followed by proteolytic removal of the C-terminal three amino acids and methylation of the free carboxyl group of cysteine (2,15,22).In mammals and the yeast Saccharomyces cerevisiae, protein FTase is a heterodimeric enzyme composed of an ␣ and a ␤ subunit (the yeast subunits are designated Ram2p and Ram1p, respectively) (21,24,40,41,45). A second protein prenyltransferase, geranylgeranyltransferase type I (GGTase-I), uses geranyl...

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Protein Farnesyltransferase in Plants (Molecular Cloning and Expression of a Homolog of the [beta] Subunit from the Garden Pea)

Cited by 45 publications

References 51 publications

Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues.

Expression of the Arabidopsis HMG2 gene, encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase, is restricted to meristematic and floral tissues.

Isoprenylcysteine Methylation and Demethylation Regulate Abscisic Acid Signaling inArabidopsis

Plant Farnesyltransferase Can Restore Yeast Ras Signaling and Mating

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