Analysis of Arabidopsis thaliana transgenic plants transformed with CER2 and CER3 genes in sense and antisense orientations

Eisner, Galina; Negruk, V. I.; Hannoufa, Abdelali; Lemieux, Bertrand

doi:10.1007/s001220050959

Cited by 3 publications

(4 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our genetic and biochemical data clearly show that PRT6 is not identical with the previously described CER3 gene. Hannoufa et al [19] presented the sequence http://X95962 (corresponding to the carboxyl‐terminal half of PRT6) as the CER3 gene, and work from the same group confirmed in a follow‐up study that sequences of the 3’ half of the PRT6 gene can complement a cer3 mutation [20]. However, the cer3‐1 mutation was mapped to the bottom arm of chromosome 5 [21], whereas PRT6 is located at the top of this chromosome.…”

Section: Discussionmentioning

confidence: 99%

“…In this work, we investigated the function of locus At5g02310, which encodes the Arabidopsis protein most similar to yeast N‐end rule ligase Ubr1. Previous studies annotated this locus as ECERIFERUM 3 ( CER3 ), a gene essential for epicuticular wax biosynthesis [19,20]. cer mutants [21] are most easily identified by the glossy green color of their stems, because they lack the whitish layer of protective surface wax crystals.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N‐end rule pathway with arginine specificity and is not the CER3 locus

et al. 2007

View full text Add to dashboard Cite

The eukaryotic N-end rule pathway mediates ubiquitin-and proteasome-dependent turnover of proteins with a bulky amino-terminal residue. Arabidopsis locus At5g02310 shows significant similarity to the yeast N-end rule ligase Ubr1. We demonstrate that At5g02310 is a ubiquitin ligase and mediates degradation of proteins with amino-terminal Arg residue. Unlike Ubr1, the Arabidopsis protein does not participate in degradation of proteins with amino-terminal Phe or Leu. This modified target specificity coincides with characteristic differences in domain structure. In contrast to previous publications, our data indicate that At5g02310 is not identical to CER3, a gene involved in establishment of a protective surface wax layer. At5g02310 has therefore been re-designated PROTEOLYSIS 6 (PRT6), in accordance with its ubiquitin ligase function.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N‐end rule pathway with arginine specificity and is not the CER3 locus

et al. 2007

View full text Add to dashboard Cite

show abstract

“…In their 1996 paper, Hannoufa et al [21] reported the identification of the CER3 gene (GenBank accession X95962) and in a subsequent publication the same researchers [32] showed that the cer3 mutation can be complemented with the corresponding gene. However, upon completion of the Arabidopsis genome sequence for chromosome 5 it became apparent that the chromosomal location of X95962 corresponding to the At5g02310 gene does not match the previously determined location of the cer3‐1 mutation on the genetic map [27,28].…”

Section: Discussionmentioning

confidence: 99%

The CER3 wax biosynthetic gene from Arabidopsis thaliana is allelic to WAX2/YRE/FLP1

et al. 2007

View full text Add to dashboard Cite

The cuticle coats the aerial organs of land plants and is composed of a cutin matrix embedded and overlayed with waxes. The Arabidopsis CER3 gene is important for cuticular wax biosynthesis and was reported to correspond to At5g02310 encoding an E3 ubiquitin ligase. Here, we demonstrate that CER3 is not At5g02310 and instead corresponds to WAX2/ YRE/FLP1 (At5g57800), a gene of unknown function required for wax biosynthesis. CER3 protein has also been implicated in cutin production because strong cer3 alleles display organ fusions. Leaf cutin analysis of two cer3 alleles did not reveal significant differences in cutin load or composition, indicating that CER3 has no major role in leaf cutin formation.

show abstract

“…Therefore, the effects of CER2-LIKE proteins on the final steps of VLCFA elongation have an important effect on the structure and physical properties of the cuticle. Male sterility dependent on humidity of the environment is a phenotype associated with pollen coat deficiencies, and has been observed in several Arabidopsis mutants with deficiencies in cuticular wax metabolism (Koornneef et al, 1989;Preuss et al, 1993) including one cer2 allele (Preuss et al, 1993;Eisner et al, 1998). The most abundant acyl lipids in the pollen coat are C29 alkane, C29 ketone, and C31 alkene (Jessen et al, 2011), and so it is not surprising that the biosynthesis of cuticular waxes and pollen coat could require the same or similar enzymes.…”

Section: Modification Of Fae1-type Kcs Specificity By Cer2-likes Is Omentioning

confidence: 99%

ECERIFERUM2-LIKE Proteins Have Unique Biochemical and Physiological Functions in Very-Long-Chain Fatty Acid Elongation

et al. 2015

View full text Add to dashboard Cite

The extension of very-long-chain fatty acids (VLCFAs) for the synthesis of specialized apoplastic lipids requires unique biochemical machinery. Condensing enzymes catalyze the first reaction in fatty acid elongation and determine the chain length of fatty acids accepted and produced by the fatty acid elongation complex. Although necessary for the elongation of all VLCFAs, known condensing enzymes cannot efficiently synthesize VLCFAs longer than 28 carbons, despite the prevalence of C28 to C34 acyl lipids in cuticular wax and the pollen coat. The eceriferum2 (cer2) mutant of Arabidopsis (Arabidopsis thaliana) was previously shown to have a specific deficiency in cuticular waxes longer than 28 carbons, and heterologous expression of CER2 in yeast (Saccharomyces cerevisiae) demonstrated that it can modify the acyl chain length produced by a condensing enzyme from 28 to 30 carbon atoms. Here, we report the physiological functions and biochemical specificities of the CER2 homologs CER2-LIKE1 and CER2-LIKE2 by mutant analysis and heterologous expression in yeast. We demonstrate that all three CER2-LIKEs function with the same small subset of condensing enzymes, and that they have different effects on the substrate specificity of the same condensing enzyme. Finally, we show that the changes in acyl chain length caused by each CER2-LIKE protein are of substantial importance for cuticle formation and pollen coat function.

show abstract

Analysis of Arabidopsis thaliana transgenic plants transformed with CER2 and CER3 genes in sense and antisense orientations

Cited by 3 publications

References 25 publications

PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N‐end rule pathway with arginine specificity and is not the CER3 locus

PRT6/At5g02310 encodes an Arabidopsis ubiquitin ligase of the N‐end rule pathway with arginine specificity and is not the CER3 locus

The CER3 wax biosynthetic gene from Arabidopsis thaliana is allelic to WAX2/YRE/FLP1

ECERIFERUM2-LIKE Proteins Have Unique Biochemical and Physiological Functions in Very-Long-Chain Fatty Acid Elongation

Contact Info

Product

Resources

About