MOESM1 of Production of xylooligosaccharides and monosaccharides from poplar by a two-step acetic acid and peroxide/acetic acid pretreatment

Additional file 1: Table S1. The AC concentration and recovery of AC pretreatment liquor. Figure S1. XRD analysis of raw and two steps treated. Figure S2. FT-IR spectrum of raw and two steps pretreated poplar. Figure S3. XPS analysis of raw and two steps pretreated poplar. Figure S4. Hydrophobicity of raw and two steps pretreated poplar. Figure S5. SEM analysis of raw and two steps pretreated poplar. Figure S6. Effect of CTec2 loading on the hydrolysis of poplar (2%) pretreated by AC (5%, 170 °C, 30 min) for 48 h

Rolling Up Gold Nanoparticle-Dressed DNA Origami into Three-Dimensional Plasmonic Chiral Nanostructures

Construction of three-dimensional (3D) plasmonic architectures using structural DNA nanotechnology is an emerging multidisciplinary area of research. This technology excels in controlling spatial addressability at sub-10 nm resolution, which has thus far been beyond the reach of traditional top-down techniques. In this paper, we demonstrate the realization of 3D plasmonic chiral nanostructures through programmable transformation of gold nanoparticle (AuNP)-dressed DNA origami. AuNPs were assembled along two linear chains on a two-dimensional rectangular DNA origami sheet with well-controlled positions and particle spacing. By rational rolling of the 2D origami template, the AuNPs can be automatically arranged in a helical geometry, suggesting the possibility of achieving engineerable chiral nanomaterials in the visible range

<i>osa</i> mutations do not disrupt GSC maintenance in the ovary.

<p><i>osa</i> mutations do not disrupt GSC maintenance in the ovary.</p

<i>brm</i> genetically interacts with <i>bap180</i> but not <i>osa</i> in maintaining GSCs.

<p>*<i>p</i><0.05.</p

Evidence for Chromatin-Remodeling Complex PBAP-Controlled Maintenance of the <i>Drosophila</i> Ovarian Germline Stem Cells

<div><p>In the <i>Drosophila</i> oogenesis, germline stem cells (GSCs) continuously self-renew and differentiate into daughter cells for consecutive germline lineage commitment. This developmental process has become an <i>in vivo</i> working platform for studying adult stem cell fate regulation. An increasing number of studies have shown that while concerted actions of extrinsic signals from the niche and intrinsic regulatory machineries control GSC self-renewal and germline differentiation, epigenetic regulation is implicated in the process. Here, we report that Brahma (Brm), the ATPase subunit of the <i>Drosophila</i> SWI/SNF chromatin-remodeling complexes, is required for maintaining GSC fate. Removal or knockdown of Brm function in either germline or niche cells causes a GSC loss, but does not disrupt normal germline differentiation within the germarium evidenced at the molecular and morphological levels. There are two <i>Drosophila</i> SWI/SNF complexes: the Brm-associated protein (BAP) complex and the polybromo-containing BAP (PBAP) complex. More genetic studies reveal that mutations in <i>polybromo</i>/<i>bap180</i>, rather than gene encoding Osa, the BAP complex-specific subunit, elicit a defect in GSC maintenance reminiscent of the <i>brm</i> mutant phenotype. Further genetic interaction test suggests a functional association between <i>brm</i> and <i>polybromo</i> in controlling GSC self-renewal. Taken together, studies in this paper provide the first demonstration that Brm in the form of the PBAP complex functions in the GSC fate regulation.</p></div

Mutation or reduced expression of <i>brm</i> or <i>polybromo/bap180</i> in the germline causes a defective GSC maintenance.

<p>(A, A′) In the wild type germarium, <i>brm</i> is ubiquitously expressed in almost all cell types, predominantly in TFs, CpCs, ECs and follicle cells (FCs). (B–I) Germaria with the control (B, C, F, G) or <i>brm^T362</i> (D, E) or <i>bap180^Δ86</i> (H, I) mutant GSC clones (broken circles) marked by the absence of GFP and the presence of an anteriorly anchored spectrosome (α-spectrin staining). In the wild type controls, marked GSCs are evident at 2 days and 14 days ACI (B, C, F, G). Conversely, marked GSCs mutant for <i>brm</i> (D) or <i>bap180</i> (H) are only detected at 2 days ACI, but lost at 14 days ACI (E, I). Instead, the mutant cyst clones are present in the germaria (arrows in E and I). (J, K) The control (J) and <i>brm</i> knockdown (K) germarium stained for α-spectrin and Vasa. While two GSCs are present in the control germarium, the mutant one contains only one GSC. GSCs are indicated by arrows. (L) Graph showing the relative percentage of germaria containing marked wild type control or <i>brm</i> or <i>bap180</i> mutant GSCs over a 3-week period ACI. Note that all initial percentages at day 2 ACI are normalized to 100%. (M) Graph showing that a gradual GSC loss is elicited by knocking down either <i>brm</i> or <i>bap180</i> in the germline.</p

Removal or knock down of <i>brm</i> or <i>bap180</i> function does not disrupt germline differentiation within the germarium.

<p>(A–J′) Germaria containing <i>brm^T362</i> (A–E′) or <i>bap180^Δ86</i> (F–J′) mutant germ cell clones (broken circles) marked by the absence of nuclear GFP, stained for Sxl (A, A′, F, F′), A2BP1 (B, B′, G, G′), Nanos (C, C′, H, H′), Bruno (D, D′, I, I′) or Orb (E, E′, J, J′). GSC-derived germline differentiation within the germarium proceeds with dynamic expression of a number of molecular markers such as Sxl in GSCs/CBs (A, A′, F, F′), A2BP1 in germ cells starting from the 4-cell cysts (B, B′, G, G′), Nanos in 16-cell germline cysts (C, C′, H, H′), Bruno in germ cells of the 16-cell cysts (D, D′, I, I′) and Orb in oocyte of the 16-cell cysts (E, E′, J, J′). The expression pattern of all tested differentiation markers remains unchanged in the germline clones homozygous for either <i>brm^T362</i> (A–E′) or <i>bap180^Δ86</i> (F–J′). (K) Graph shows that compared with the controls, <i>brm</i> knockdown in ECs does not cause the accumulation of UGCs in the germarium over a 14-day time course after eclosion.</p

Knock down of the PBAP complex subunits in the niche leads to a gradual GSC loss.

<p>(A–D) The control germaria (A, C) and mutant ones expressing <i>brm-Dominant-Negative</i> (<i>brm[K804R]</i>) (B) or <i>bap180-RNAi</i> transgene (D) under the control of <i>bab1-gal4</i>, stained for Vasa and α-spectrin. Only one GSC is present in the knockdown germarium at 14 days after eclosion (B, D), whereas the control germarium contains two GSCs (A, C). GSCs are indicated by arrows in all panels. (E, F) Graphs show that compared with the controls, knocking down <i>brm</i> (E) or the PBAP specific subunit encoding gene (<i>bap180</i> or <i>bap170</i>) (F) in the niche causes a significant drop of GSC number per germarium over a 2-week period after eclosion.</p

Effect of Dilute Acetic Acid Hydrolysis on Xylooligosaccharide Production and the Inhibitory Effect of Cellulolytic Enzyme Lignin from Poplar

Acetic acid (AC) hydrolysis has been reported to prepare xylooligosaccharides (XOS) from poplar. However, the influence of AC hydrolysis on the lignin structure changes is not clear, which is important for the following enzymatic hydrolysis of poplar. Herein, AC was used to produce XOS, and cellulase adsorption on cellulolytic enzyme lignin (CEL) from AC-hydrolyzed poplar and its inhibitory effect on two commercial cellulase preparations were investigated. AC hydrolysis gave a XOS yield of 39.8% from poplar. After AC hydrolysis at 170 °C, the hydrophobicity and ζ-potential of CEL decreased to 2.3 L/g and 14.8 mV, respectively. The adsorption strength of CTec2 on CEL samples did not increase by AC hydrolysis, and the inhibitory effect of CEL on Celluclast 1.5L and β-glucosidase was observed, but not on CTec2. CEL samples improved the lytic polysaccharide monooxygenase (LPMO) activity of the enzymatic hydrolysis by CTec2. After CEL samples were added in enzymatic hydrolysis, the free filter paper activity of Celluclast 1.5L and β-G retained in the enzymatic hydrolysate decreased from 60.5 to 29.3–42.9%. The addition of CEL samples in enzymatic hydrolysis could not decrease the free filter paper activity of CTec2 retained in the enzymatic hydrolysate. In the enzymatic hydrolysis with CEL samples, higher glucose yields were obtained by CTec2 than those by Celluclast 1.5L and β-glucosidase. This work will help to understand the structure and inhibitory effects of AC-CELs and guide the development of AC hydrolysis for the production of XOS and monosaccharides from poplar

Table_1_The discovery and characterization of AeHGO in the branching route from shikonin biosynthesis to shikonofuran in Arnebia euchroma.xlsx

Shikonin derivatives are natural naphthoquinone compounds and the main bioactive components produced by several boraginaceous plants, such as Lithospermum erythrorhizon and Arnebia euchroma. Phytochemical studies utilizing both L. erythrorhizon and A. euchroma cultured cells indicate the existence of a competing route branching out from the shikonin biosynthetic pathway to shikonofuran. A previous study has shown that the branch point is the transformation from (Z)-3’’-hydroxy-geranylhydroquinone to an aldehyde intermediate (E)-3’’-oxo-geranylhydroquinone. However, the gene encoding the oxidoreductase that catalyzes the branch reaction remains unidentified. In this study, we discovered a candidate gene belonging to the cinnamyl alcohol dehydrogenase family, AeHGO, through coexpression analysis of transcriptome data sets of shikonin-proficient and shikonin-deficient cell lines of A. euchroma. In biochemical assays, purified AeHGO protein reversibly oxidized (Z)-3’’-hydroxy-geranylhydroquinone to produce (E)-3’’-oxo-geranylhydroquinone followed by reversibly reducing (E)-3’’-oxo-geranylhydroquinone to (E)-3’’-hydroxy-geranylhydroquinone, resulting in an equilibrium mixture of the three compounds. Time course analysis and kinetic parameters showed that the reduction of (E)-3’’-oxo-geranylhydroquinone was stereoselective and efficient in presence of NADPH, which determined that the overall reaction proceeded from (Z)-3’’-hydroxy-geranylhydroquinone to (E)-3’’-hydroxy-geranylhydroquinone. Considering that there is a competition between the accumulation of shikonin and shikonofuran derivatives in cultured plant cells, AeHGO is supposed to play an important role in the metabolic regulation of the shikonin biosynthetic pathway. Characterization of AeHGO should help expedite the development of metabolic engineering and synthetic biology toward production of shikonin derivatives.</p