<i>P</i>‑Chiral Phosphine–Sulfonate/Palladium-Catalyzed Asymmetric Copolymerization of Vinyl Acetate with Carbon Monoxide

Utilization of palladium catalysts bearing a <i>P</i>-chiral phosphine–sulfonate ligand enabled asymmetric copolymerization of vinyl acetate with carbon monoxide. The obtained γ-polyketones have head-to-tail and isotactic polymer structures. The origin of the regio- and stereoregularities was elucidated by stoichiometric reactions of acylpalladium complexes with vinyl acetate. The present report for the first time demonstrates successful asymmetric coordination–insertion (co)­polymerization of vinyl acetate

<i>P</i>‑Chiral Phosphine–Sulfonate/Palladium-Catalyzed Asymmetric Copolymerization of Vinyl Acetate with Carbon Monoxide

Utilization of palladium catalysts bearing a <i>P</i>-chiral phosphine–sulfonate ligand enabled asymmetric copolymerization of vinyl acetate with carbon monoxide. The obtained γ-polyketones have head-to-tail and isotactic polymer structures. The origin of the regio- and stereoregularities was elucidated by stoichiometric reactions of acylpalladium complexes with vinyl acetate. The present report for the first time demonstrates successful asymmetric coordination–insertion (co)­polymerization of vinyl acetate

<i>P</i>‑Chiral Phosphine–Sulfonate/Palladium-Catalyzed Asymmetric Copolymerization of Vinyl Acetate with Carbon Monoxide

Utilization of palladium catalysts bearing a <i>P</i>-chiral phosphine–sulfonate ligand enabled asymmetric copolymerization of vinyl acetate with carbon monoxide. The obtained γ-polyketones have head-to-tail and isotactic polymer structures. The origin of the regio- and stereoregularities was elucidated by stoichiometric reactions of acylpalladium complexes with vinyl acetate. The present report for the first time demonstrates successful asymmetric coordination–insertion (co)­polymerization of vinyl acetate

Nucleotide substitution in <i>MSX1</i> gene in a family with nonsyndromic tooth agenesis.

<p>(A) Genomic sequence analysis. Electropherograms of the junction between the intronic region and exon 2 of the <i>MSX1</i> gene. Unaffected (II-1) and affected (II-2) members of the family are indicated. There was a nucleotide substitution found in the intronic region nine nucleotides before the initiation site of the second exon (c.452-9G>A indicated by arrow). All of the affected members in the pedigree had the same heterozygous c.452-9G>A mutation. Thick cylinders, exons; red cylinder, predicted additional 7-nucleotide insertion. (B) cDNA sequence analysis. Electropherograms of the junction between exons 1 and 2 of the <i>MSX1</i> cDNA isolated from the lymphoblastoid cell lines generated from the proband (III-1). The 7-bp insertion is shown in the box.</p

Pedigree and panoramic X-ray photograph.

<p>(A) Pedigree affected by nonsyndromic oligodontia. The pedigree displays an autosomal dominant mode of inheritance. Squares indicate males and circles indicate females. Black and white symbols indicate affected and unaffected individuals, respectively. The arrow indicates the proband, III-1. Asterisks indicate individuals analyzed by whole-exome sequencing. Mut, c.452-9G>A; wt, wild-type. (B) Panoramic X-ray (upper panel) and the missing tooth pattern (lower panel) of the proband (III-1).</p

Sequence of cDNA generated by minigene.

<p>(A) Schematic diagram of the FLAG-tagged <i>MSX1</i> gene. Thick cylinders, exons; blue cylinder, FLAG-tag; asterisk, position at nucleotide substitution; red cylinder, 7-nucleotide insertion. (B) Electropherograms of the <i>MSX1</i> cDNA isolated from the COS7 cells transfected with <i>MSX1</i> minigene plasmids; wild-type (II-1) and c.452-9G>A (II-2). (C) Predicted amino acid sequences of wild-type (upper) and p.R151fsX20 (lower). The 7-bp insertion and 19 additional amino acids residues in the C-terminus are highlighted in red.</p

Characterization of the gene product of the <i>MSX1</i> gene with the c.452-9G>A substitution.

<p>(A) Immunolocalization of FLAG-tagged MSX1 protein in transfected COS7 cells. Nuclear translocation (wild-type) is disrupted by c.452-9G>A substitution in the intronic region (mutant). A diffuse signal is also observed in the transfectant of W139X MSX1, which is a C-terminal truncated mutant. (B) Schematic repetitions of wild and mutant MSX1 protein. The mutant MSX1 protein lacks the homeodomain (green cylinder in wild-type MSX1). Blue cylinder, FLAG tag; red cylinder, unrelated peptide generated by the insertion caused by the c.452-9G>A substitution. (C) Western blotting of cell lysate prepared from total cells (left) or nuclear fractions (right) of COS7 transfected with the <i>MSX1</i> minigene (FLAG tagged wild-type and c.452-9G>A) or cDNA (FLAG tagged wild-type and W139X) expression vectors. The molecular masses of the R151fsX20 and W139X MSX1 proteins are lower than that of wild-type MSX1.</p

Additional file 1: of Bivalve-specific gene expansion in the pearl oyster genome: implications of adaptation to a sessile lifestyle

Table S1. Summary of Pinctada fucata genome sequence data. Table S2. Summary of the Pinctada fucata genome assemblies. Table S3. Numbers of genes containing functional domains related to heat shock proteins. See also Fig. 3a. Table S4. Numbers of genes containing functional domains related to non-self recognition and signaling. See also Fig. 4a. Table S5. List of biomineralization-related genes tandemly arranged in the genome. See also Fig. 5. Table S6. Hox and neighboring gene models tandemly arranged in the genome. Table S7. ParaHox and neighboring gene models tandemly arranged in the genome. Table S8. Wnt and adjacent gene models tandemly arranged in the genome. (PDF 385 kb