An Enantiocomplementary Dirigent Protein for the Enantioselective Laccase‐Catalyzed Oxidative Coupling of Phenols

Pickel, Benjamin; Constantin, Mihaela‐Anca; Pfannstiel, Jens; Conrad, Jürgen; Beifuß, Uwe; Schaller, Andreas

doi:10.1002/anie.200904622

Cited by 150 publications

(102 citation statements)

References 25 publications

(20 reference statements)

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“…The DIR protein led to the production of (+)-pinoresinol, a type of lignan, instead of a mixture of three racemic dimeric compounds (dilignols), including (±)-pinoresinol. The mediation of stereoselective coupling with DIR proteins has also been reported in moco cotton (35) and Arabidopsis (36,37). Despite the presence of many genes encoding this protein family in vascular plants (26,38), their only suggested role in planta was related to disease resistance (28, 39) until Hosmani et al (40) reported the essential role of a dirigent domain-containing protein, ESB1, in the formation of lignin-based Casparian strips in roots.…”

Section: Discussionmentioning

confidence: 96%

Molecular basis of a shattering resistance boosting global dissemination of soybean

Funatsuki

Suzuki

Hirose

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

184

223

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Pod dehiscence (shattering) is essential for the propagation of wild plant species bearing seeds in pods but is a major cause of yield loss in legume and crucifer crops. Although natural genetic variation in pod dehiscence has been, and will be, useful for plant breeding, little is known about the molecular genetic basis of shattering resistance in crops. Therefore, we performed map-based cloning to unveil a major quantitative trait locus (QTL) controlling pod dehiscence in soybean. Fine mapping and complementation testing revealed that the QTL encodes a dirigent-like protein, designated as Pdh1. The gene for the shattering-resistant genotype, pdh1, was defective, having a premature stop codon. The functional gene, Pdh1, was highly expressed in the lignin-rich inner sclerenchyma of pod walls, especially at the stage of initiation in lignin deposition. Comparisons of near-isogenic lines indicated that Pdh1 promotes pod dehiscence by increasing the torsion of dried pod walls, which serves as a driving force for pod dehiscence under low humidity. A survey of soybean germplasm revealed that pdh1 was frequently detected in landraces from semiarid regions and has been extensively used for breeding in North America, the world's leading soybean producer. These findings point to a new mechanism for pod dehiscence involving the dirigent protein family and suggest that pdh1 has played a crucial role in the global expansion of soybean cultivation. Furthermore, the orthologs of pdh1, or genes with the same role, will possibly be useful for crop improvement.

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Section: Discussionmentioning

confidence: 96%

Molecular basis of a shattering resistance boosting global dissemination of soybean

Funatsuki

Suzuki

Hirose

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

184

223

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“…AtDIR6 is a glycoprotein carrying N-linked paucimannosetype glycans at Asn-59 and Asn-123 that are required for protein solubility and function (Pickel et al, 2010;Kazenwadel et al, 2013). Glycans at Asn-59 are well ordered (Supplemental Fig.…”

Section: Overall Structurementioning

confidence: 99%

“…S1B). Apparently, since the signal peptide was shown to be cleaved between residues 29 and 30 (Pickel et al, 2010), additional processing resulted in the loss of three more amino acids (residues 30-32) from the N terminus of the protein. In monomer A, the first two residues, Thr-33 and Ile-34, are disordered and, thus, not resolved in the structure.…”

Section: Overall Structurementioning

confidence: 99%

“…First support for a more general contribution of DIRs to stereoselective natural product formation was provided by AtDIR6 from Arabidopsis (Pickel et al, 2010). AtDIR6 acts on the same substrate as FiDIR1 but directs the coupling reaction toward (2)-rather than (+)-pinoresinol (Pickel et al, 2010;Kazenwadel et al, 2013).…”

mentioning

confidence: 99%

“…AtDIR6 acts on the same substrate as FiDIR1 but directs the coupling reaction toward (2)-rather than (+)-pinoresinol (Pickel et al, 2010;Kazenwadel et al, 2013). In addition to the prototypical FiDIR1 and AtDIR6, further (+)-and (2)-pinoresinol-forming DIRs have been identified in several other plant species (Davin and Lewis, 2005a;Kim et al, 2012;Dalisay et al, 2015;Seneviratne et al, 2015).…”

mentioning

confidence: 99%

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Dirigent Protein Mode of Action Revealed by the Crystal Structure of AtDIR6

et al. 2016

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Dirigent proteins impart stereoselectivity to phenoxy radical coupling reactions in plants and, thus, play an essential role in the biosynthesis of biologically active natural products. This includes the regioselective and enantioselective coupling and subsequent cyclization of two coniferyl alcohol radicals to pinoresinol as the committed step of lignan biosynthesis. The reaction is controlled by dirigent proteins, which, depending on the species and protein, direct the reaction to either (+)-or (2)-pinoresinol. We present the crystal structure of the (2)-pinoresinol forming DIRIGENT PROTEIN6 (AtDIR6) from Arabidopsis (Arabidopsis thaliana) with data to 1.4 Å resolution. The structure shows AtDIR6 as an eight-stranded antiparallel b-barrel that forms a trimer with spatially well-separated cavities for substrate binding. The binding cavities are two lobed, exhibiting two opposing pockets, each lined with a set of hydrophilic and potentially catalytic residues, including essential aspartic acids. These residues are conserved between (+) and (2)-pinoresinol-forming DIRs and required for activity. The structure supports a model in which two substrate radicals bind to each of the DIR monomers. With the aromatic rings fixed in the two pockets, the propionyl side chains face each other for radical-radical coupling, and stereoselectivity is determined by the exact positioning of the side chains. Extensive mutational analysis supports a previously unrecognized function for DIRs in catalyzing the cyclization of the bis-quinone methide reaction intermediate to yield (+)-or (2)-pinoresinol.

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