Experimental parameters.

<p>Experimental parameters.</p

Influence of different settlement-inducing cues and exposure times on gene expression of <i>Acropora millepora</i> larvae.

<p>PCA score plots of the % difference in gene expression compared to the control, presented with convex hulls highlighting groupings and showing PC1 and PC2, for A) J010-E 1–12 hpi and HO_org/aq, Assay 1, B) J010-E 1–12 hpi and HO_org/aq, Assay 2, C) J010-E 1–12 hpi, Assay 1, D) J010-E 1–12 hpi, Assay 2, E) HO_org/aq, Assay 1 and F) HO_org/aq, Assay 2. Time points for J010-E are represented by: 1 hpi = black full circle, 2 hpi = blue empty square, 3 hpi = green empty circle and 12 hpi = cyan empty triangle. CCA-derived cues are represented by: HO_org = pink full square and HO_aq = red cross.</p

Differential gene expression following exposure to bacteria- and CCA-derived cues.

<p>Significant (<i>p<0.05</i>) change in gene regulation is given as the % difference compared to the control. Dark and light green (+) represents those genes that were up-regulated (X>20, 20≤X<0); orange and red (−) represents those that were down-regulated (0>X≥−20, X<−20). Data from the 12 hpi experiment (high concentration treatment and complete metamorphosis) was taken from Siboni et al. <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0091082#pone.0091082-Siboni1" target="_blank">[12]</a>, which also includes full protein names and description of the genes.</p

Schematic diagram of electron transfer reactions using the coenzyme Q (CoQ) pool in the coral mitochondrial and plasma membrane electron transport.

<p>Respiratory “linear” electron flows (black arrows) proceed from NADH in the mitochondrial matrix to H₂O via the CoQ pool and the enzyme complexes I, II, III, and IV, forming ubiquinol (CoQH₂) as an intermediary product. The electron flows via complexes I, III and IV occur (mostly) via tunnelling or micro-diffusion of CoQ/CoQH₂ in I-II-IV supercomplexes rather than via the larger mobile CoQ pool [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0139290#pone.0139290.ref072" target="_blank">72</a>]. “Non-linear” electron flows (dark blue arrows) proceed from electron donors (e.g. NAD(P)H) via several quinone dehydrogenases to the CoQ pool, and to H₂O from CoQH₂ via AOX. Plasma membrane electron transport occurs from NAD(P)H to H₂O via one or more type of NAD(P)H-CoQ reductases, the plasma membrane CoQ pool and Ecto-NOX. CoQH₂ ROS scavenging occurs continuously in O₂ metabolism primarily via chain breaking of lipid peroxidation (LPO) caused by O₂^•− and H₂O₂. Abbreviations: AOX, alternative oxidase; cyt-c, cytochrome c; DHAP, dihydroxyacetone phosphate; DHO, dihydroorotate; DHODH, dihydroorotate dehydrogenase; Ecto-NOX, external quinone oxidase; ETF_red/ox, reduced/oxidised electron-transferring-flavoprotein; ETFDH, electron-transferring-flavoprotein dehydrogenase reduced/oxidised; Ecto-NOX, external quinone oxidase; GPDH, glycerol-3-phosphate dehydrogenase; G-3-P, glycerol-3-phosphate; H₂O₂, hydrogen peroxide_; LPO, lipid peroxidation; pmNDH/mNDH, plasma membrane/mitochondrial NAD(P)H dehydrogenases; OA, orotate; O₂^•−, superoxide.</p

Representative transmission electron micrographs documenting the effects of thermal stress on the internal structure of endosymbiotic <i>Symbiodinium</i> cells within tissue of <i>Acropora millepora</i>.

<p>(A) <i>Symbiodinium</i> exposed to 27°C showing intact organelles and thylakoid membranes (black arrow). (B) First signs of degraded internal structures in some <i>Symbiodinium</i> cells after 7 days of heat stress (white arrows). Note the intact structure of the thylakoid membranes (black arrow). (C and D) <i>Symbiodinium</i> exposed to 32°C revealing degraded internal structures (white arrows). Scale bars, 1 μm; ch, chloroplast; nu, nucleus.</p

Effects of thermal stress on physiological parameters of the scleractinian coral <i>Acropora millepora</i>.

<p>Images of representative coral nubbins demonstrating the visual difference in <i>Symbiodinium</i> cell densities within <i>A</i>. <i>millepora</i> tissues under control (27°C) (A—B) and thermal stress (32°C) (C—D) conditions at day 17 (end of experiment). Scale bars = 1 mm. Thermal stress effects on (E) <i>Symbiodinium</i> density; (F) photosystem II photochemical efficiency; (G) plastoquinone (%PQH₂) and (H) coenzyme Q (%CoQH₂) pool redox states; (I) total plastoquinone concentration (PQ + PQH₂) per <i>Symbiodinium</i> cell and (J) total coenzyme Q concentration (CoQ + CoQH₂) per coral surface area over the course of the experiment. All data points are means ± 95% CI; * indicate significant differences between control and treatment at <i>p</i> < 0.05; <i>n</i> = 6–12 (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0139290#pone.0139290.t001" target="_blank">Table 1</a> for details).</p

Temperature logger data for the experimental period.

<p>Thermal log of the four temperature sensors placed in heated (32°C) and control (27°C) seawater aquarium tanks for the duration of the experimental period. Two temperature sensors were used per treatment. Dashed lines indicate sampling time points.</p

Linear mixed model testing for differences in temperature treatments (27°C = control; 32°C = stress) during a hyperthermal bleaching experiment of <i>Acropora millepora</i> containing <i>Symbiodinium</i> type C2.

<p>CoQ, coenzyme Q; %CoQH₂, coenzyme Q pool redox state; F_V/F_M, maximum quantum yield; PQ, plastoquinone; %PQH₂, plastoquinone pool redox state.</p><p>^a F_V/F_M was measured daily (18 time points), other measurements at four time points.</p><p>^b,c replication number given is for the full set. Due to dropouts, for the last time point <i>n</i> = 10 (^b) and <i>n</i> = 8 (^c).</p><p><i>p</i>-values significant at α < 0.05 are highlighted in boldface.</p><p>Linear mixed model testing for differences in temperature treatments (27°C = control; 32°C = stress) during a hyperthermal bleaching experiment of <i>Acropora millepora</i> containing <i>Symbiodinium</i> type C2.</p

Accelerated Identification of Halogenated Monoterpenes from Australian Specimens of the Red Algae <i>Plocamium hamatum</i> and <i>Plocamium costatum</i>

Two species of red algae belonging to the genus <i>Plocamium</i>, <i>P. hamatum</i> from Moreton Bay, Queensland, and <i>P. costatum</i>, from Pandalowie Bay, South Australia, were investigated to assess their chemical variation and as potential sources of new halogenated monoterpenes. The hyphenated technique HPLC-UV-MS-SPE-NMR was used to assess the algal extracts and to determine its potential for accelerated identification of halogenated monoterpenes generally. A combination of the hyphenated and traditional chromatographic techniques resulted in the isolation and characterization of a total of 10 halogenated monoterpene metabolites, eight of which are reported for the first time. Their structures, including configurations, were determined through interpretation of their 1D and 2D NMR, mass spectrometric, infrared, and X-ray data. The two species of <i>Plocamium</i> produced different secondary metabolites and contained a significant number of new polyhalogenated monoterpenes. The investigation also showed the hyphenated technique HPLC-UV-MS-SPE-NMR to be useful for preliminary investigation of the chemical content of algal extracts

Post-Assembly Covalent Di- and Tetracapping of a Dinuclear [Fe₂L₃]⁴⁺ Triple Helicate and Two [Fe₄L₆]⁸⁺ Tetrahedra Using Sequential Reductive Aminations

The use of a highly efficient reductive amination procedure for the postsynthetic end-capping of metal-templated helicate and tetrahedral supramolecular structures bearing terminal aldehyde groups is reported. Metal template formation of a [Fe₂L₃]⁴⁺ dinuclear helicate and two [Fe₄L₆]⁸⁺ tetrahedra (where L is a linear ligand incorporating two bipyridine domains separated by one or two 1,4-(2,5-dimethoxyaryl) linkers and terminated by salicylaldehyde functions is described. Postassembly reaction of each of these “open” di- and tetranuclear species with excess ammonium acetate (as a source of ammonia) and sodium cyanoborohydride results in a remarkable reaction sequence whereby the three aldehyde groups terminating each end of the helicate, or each of the four vertices of the respective tetrahedra, react with ammonia then undergo successive reductive amination to yield corresponding fully tertiary-amine capped cryptate and tetrahedral covalent cages