<i>Arabidopsis thaliana</i>
            defense-related protein ELI3 is an aromatic alcohol:NADP
            <sup>+</sup>
             oxidoreductase

Somssich, Imre E.; Wernert, Petra; Kiedrowski, Siegrid; Hahlbrock, Klaus

doi:10.1073/pnas.93.24.14199

Cited by 80 publications

(71 citation statements)

References 33 publications

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“…Genes involved in monolignol precursor biosynthesis are found, including genes encoding 4-coumarate CoA ligase (4CL, contig 1516 in Table 1) and caffeoylCoA O-methyltransferase (CCoAOMT, contig 1539 in Table 1). Other genes of less certain relationship to lignin biosynthesis are also highly expressed, such as a gene (contig 1524) very similar to ELI3 of parsley, which encodes a protein with benzyl alcohol dehydrogenase activity (Somssich et al, 1996). At least one transcript encoding a protein similar to laccase is highly abundant, while none of the abundant transcripts encode peroxidases, consistent with findings of pilot-scale EST studies of pine and poplar (Allona et al, 1998;Sterky et al, 1998;Mellerowicz et al, 2001, this issue).…”

Section: What Types Of Genes Are Abundantly Expressed In Wood-formingsupporting

confidence: 70%

Functional genomics and cell wall biosynthesis in loblolly pine

et al. 2001

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Loblolly pine (Pinus taeda L.) is the most widely planted tree species in the USA and an important tree in commercial forestry world-wide. The large genome size and long generation time of this species present obstacles to both breeding and molecular genetic analysis. Gene discovery by partial DNA sequence determination of cDNA clones is an effective means of building a knowledge base for molecular investigations of mechanisms governing aspects of pine growth and development, including the commercially relevant properties of secondary cell walls in wood. Microarray experiments utilizing pine cDNA clones can be used to gain additional information about the potential roles of expressed genes in wood formation. Different methods have been used to analyze data from first-generation pine microarrays, with differing degrees of success. Disparities in predictions of differential gene expression between cDNA sequencing experiments and microarray experiments arise from differences in the nature of the respective analyses, but both approaches provide lists of candidate genes which should be further investigated for potential roles in cell wall formation in differentiating pine secondary xylem. Some of these genes seem to be specific to pine, while others also occur in model plants such as Arabidopsis, where they could be more efficiently investigated.

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Section: What Types Of Genes Are Abundantly Expressed In Wood-formingsupporting

confidence: 70%

Functional genomics and cell wall biosynthesis in loblolly pine

et al. 2001

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“…The AtCAD-B paralogs corresponding to ELI-3 proteins have been studied previously and were originally identified as part of the defense response in parsley (Petroselinum crispum) and in Arabidopsis (Kiedrowski et al, 1992). Williamson et al (1995) and Somssich et al (1996) demonstrated that ELI-3 was neither a CAD nor a malate dehydrogenase but rather a benzyl alcohol dehydrogenase, which accepts various benzaldehyde substrates. In our phylogenetic analysis, these proteins (AtCAD-A, AtCAD-B1, and -B2) fall within the same cluster as PtSAD, which has been recently identified and characterized in poplar (Li et al, 2001).…”

Section: Atcad-c and Atcad-d Belong To A Small Multigene Family In Armentioning

confidence: 99%

“…However, in most cases, these experiments led to conflicting results. Meanwhile, subsequent in depth analysis suggested unsuspected functions for these proteins (Somssich et al, 1996;Goffner et al, 1998). Together, these studies indicate that, if heterologous protein expression is useful in determining biochemical profiles, other approaches are needed to confirm a biological function.…”

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confidence: 99%

Expression Pattern of Two Paralogs Encoding Cinnamyl Alcohol Dehydrogenases in Arabidopsis. Isolation and Characterization of the Corresponding Mutants

et al. 2003

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Studying Arabidopsis mutants of the phenylpropanoid pathway has unraveled several biosynthetic steps of monolignol synthesis. Most of the genes leading to monolignol synthesis have been characterized recently in this herbaceous plant, except those encoding cinnamyl alcohol dehydrogenase (CAD). We have used the complete sequencing of the Arabidopsis genome to highlight a new view of the complete CAD gene family. Among nine AtCAD genes, we have identified the two distinct paralogs AtCAD-C and AtCAD-D, which share 75% identity and are likely to be involved in lignin biosynthesis in other plants. Northern, semiquantitative restriction fragment-length polymorphism-reverse transcriptase-polymerase chain reaction and western analysis revealed that AtCAD-C and AtCAD-D mRNA and protein ratios were organ dependent. Promoter activities of both genes are high in fibers and in xylem bundles. However, AtCAD-C displayed a larger range of sites of expression than AtCAD-D. Arabidopsis null mutants (Atcad-D and Atcad-C) corresponding to both genes were isolated. CAD activities were drastically reduced in both mutants, with a higher impact on sinapyl alcohol dehydrogenase activity (6% and 38% of residual sinapyl alcohol dehydrogenase activities for Atcad-D and Atcad-C, respectively). Only Atcad-D showed a slight reduction in Klason lignin content and displayed modifications of lignin structure with a significant reduced proportion of conventional S lignin units in both stems and roots, together with the incorporation of sinapaldehyde structures ether linked at C␤. These results argue for a substantial role of AtCAD-D in lignification, and more specifically in the biosynthesis of sinapyl alcohol, the precursor of S lignin units.Lignin is a complex phenolic polymer whose structure is vital to functions such as imparting rigidity to plant organs and as a physical barrier to invading pests. Its presence in cell wall confers to vessels hydrophobic properties that facilitate conduction of water, photo-assimilates, and minerals to different parts of the plant. Lignin structure and composition differ widely at the interspecies level as well as cell types and at the subcellular cell wall level (Donaldson, 2001). Striking differences are mostly observable between gymnosperms and angiosperms. These taxa contain different qualitative and quantitative proportions of monolignols or cinnamyl alcohols representing the main lignin monomers. The formation of cinnamyl alcohols from the corresponding cinnamoylCoA esters requires two enzymatic modifications of the carbonate chain of the phenolic precursors. The first step is catalyzed by cinnamoyl CoA reductase, and the second step is catalyzed by cinnamyl alcohol dehydrogenase (CAD). CAD leads to the conversion of hydroxy-cinnamaldehydes to the corresponding alcohols. The relative proportions of these cinnamyl alcohols is an important factor for lignin structural traits and mechanical properties (Baucher et al., 1998;Mellerowicz et al., 2001).CAD was one of the first enzymes studied in the lignin syn...

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“…Comparison of the activity profile of M. bovis BCG ADH with those of defence-related (A. thaliana ELI3±2 and P. crispum CAD) and lignification-related (E. gunnii CAD) CADs lead to interesting observations. Firstly, as observed with the M. bovis BCG ADH, processing of alcohols by defence CADs was far less efficient than that of aldehydes as shown by the 50±100-fold decrease in k cat /K m values with A. thaliana ELI3-2 [35] and the absence of alcohol dehydrogenase activity with P. crispum CAD [37]. In contrast, the k cat /K m values of E. gunnii CAD with alcohols were only 2±10-fold lower than those recorded with their corresponding aldehydes [16].…”

Section: Discussionmentioning

confidence: 94%

“…Two potential physiological functions have been attributed to the plant CADs: on one hand, there are enzymes implicated in defence reactions [35] for which the exact role is undetermined (for instance, A. thaliana ELI3±2 and P. crispum CAD) and on the other hand, there are enzymes directly involved in the biosynthesis of the lignin polymer (a cell wall component of higher plants), as exemplified by E. gunnii CAD. Lignins are formed by cell-wall peroxidases that catalyse the polymerization of three phenolic basic units, coniferyl, sinapyl and paracoumaryl alcohols depending on plant species [36].…”

Section: Discussionmentioning

confidence: 99%

Overexpression, purification and characterization of Mycobacterium bovis BCG alcohol dehydrogenase

Wilkin¹,

Soetaert²,

Stélandre³

et al. 1999

European Journal of Biochemistry

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A previous study of the effect of zinc deprivation on Mycobacterium bovis BCG pointed out the potential importance of an alcohol dehydrogenase for maintaining the hydrophobic character of the cell envelope. In this report, the effect of the overexpression of the M. bovis BCG alcohol dehydrogenase (ADH) in Mycobacterium smegmatis and M. bovis BCG is described. The purification of the enzyme was performed to apparent homogeneity from overexpressing M. bovis BCG cells and its kinetic parameters were determined. The enzyme showed a strong preference for both aromatic and aliphatic aldehydes while the corresponding alcohols were processed 100±1000-fold less efficiently. The best k cat /K m values were found with benzaldehyde . 3-methoxybenzaldehyde . octanal . coniferaldehyde. A phylogenetic analysis clearly revealed that the M. bovis BCG ADH together with the ADHs from Bacillus subtilis and Helicobacter pylori formed a sister group of the class C medium-chain alcohol dehydrogenases, the plant cinnamyl alcohol dehydrogenases (CADs). Comparison of the kinetic properties of our ADH with some related class C enzymes indicated that the mycobacterial enzyme substrate profile resembled that of the CADs involved in plant defence rather than those implicated in lignification. A possible role for the M. bovis BCG ADH in the biosynthesis of the lipids composing the mycobacterial cell envelope is proposed.Keywords: Mycobacterium bovis BCG; alcohol dehydrogenase; cinnamyl alcohol dehydrogenase.Alcohol dehydrogenases (ADHs) display a wide range of substrate specificities and fulfil several key physiological functions. They can be divided into three major categories. The first category is composed of the NAD(P)-dependent ADHs subdivided into three subgroups according to their metal dependence: (a) the medium-chain zinc-dependent enzymes; (b) the short-chain zinc-independent enzymes; and (c) the iron-activated enzymes. The NAD(P)-independent enzymes form the second category and the third category contains the oxidases which catalyse an essentially irreversible oxidation of alcohols [1].The vaccine strain Mycobacterium bovis BCG grows poorly on zinc-deprived Sauton medium, and forms a thin, pale, unfolded pellicle that gets wet and often sinks. This phenotype suggested a cell envelope with a reduced hydrophobic content. The cell composition and the products excreted into the medium, including aldehydes, can, to some extent, be correlated with a decrease of the specific activity of a soluble zinc-dependent alcohol dehydrogenase. This enzyme was partially purified from BCG cells and characterized as a dimeric NADP-dependent protein of broad specificity with higher affinities towards aldehydes than towards alcohols [2,3].The corresponding gene has been cloned and sequenced [4]. Comparison with other ADHs allowed classification of this enzyme into the zinc-containing, medium-chain alcohol/polyol dehydrogenase family which had been primarily described in eukaryotes [5]. Currently, this family is composed of the tetrameric and the dimeric...

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Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP ⁺ oxidoreductase

Cited by 80 publications

References 33 publications

Functional genomics and cell wall biosynthesis in loblolly pine

Functional genomics and cell wall biosynthesis in loblolly pine

Expression Pattern of Two Paralogs Encoding Cinnamyl Alcohol Dehydrogenases in Arabidopsis. Isolation and Characterization of the Corresponding Mutants

Overexpression, purification and characterization of Mycobacterium bovis BCG alcohol dehydrogenase

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Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP + oxidoreductase

Cited by 80 publications

References 33 publications

Functional genomics and cell wall biosynthesis in loblolly pine

Functional genomics and cell wall biosynthesis in loblolly pine

Expression Pattern of Two Paralogs Encoding Cinnamyl Alcohol Dehydrogenases in Arabidopsis. Isolation and Characterization of the Corresponding Mutants

Overexpression, purification and characterization of Mycobacterium bovis BCG alcohol dehydrogenase

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Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP ⁺ oxidoreductase