Spawning behavior of garden eels, <i>Gorgasia preclara</i> and <i>Heteroconger hassi</i> (Heterocongrinae), observed in captivity

<div><p>The behavior and reproductive ecology of typically nocturnal marine eels is poorly known but garden eels (Congridae, Heterocongrinae) are familiar tropical marine eels. They live in colonies and protrude their bodies from burrows during the daytime to feed on zooplankton. Apparent daytime courtship/spawning-like behavior has been observed within the colonies but actual spawning and fertilized egg production has not been confirmed. This study describes observations of splendid garden eels (<i>Gorgasia preclara</i>) and spotted garden eels (<i>Heteroconger hassi</i>) spawning in low light at night and producing fertilized eggs in a large multispecies public-display tank in the Sumida Aquarium. Video recordings of 5 of 17 detected spawning or egg or sperm release events documented the spawning behavior of <i>G. preclara</i>, and positively buoyant fertilized eggs of both species were collected. Their spawning behavior while protruding from widely spaced burrows confirms that garden eels likely spawn within their colonies with their pelagic eggs drifting away with currents.</p></div

Synchrotron X-ray, Photoluminescence, and Quantum Chemistry Studies of Bismuth-Embedded Dehydrated Zeolite Y

For the first time, direct experimental evidence of the formation of monovalent Bi (i.e., Bi⁺) in zeolite Y is provided based on the analysis of high-resolution synchrotron powder X-ray diffraction data. Photoluminescence results as well as quantum chemistry calculations suggest that the substructures of Bi⁺ in the sodalite cages contribute to the ultrabroad near-infrared emission. These results not only enrich the well-established spectrum of optically active zeolites and deepen the understanding of bismuth related photophysical behaviors, but also may raise new possibilities for the design and synthesis of novel hybrid nanoporous photonic materials activated by other heavier p-block elements

Synchrotron X-ray, Photoluminescence, and Quantum Chemistry Studies of Bismuth-Embedded Dehydrated Zeolite Y

For the first time, direct experimental evidence of the formation of monovalent Bi (i.e., Bi⁺) in zeolite Y is provided based on the analysis of high-resolution synchrotron powder X-ray diffraction data. Photoluminescence results as well as quantum chemistry calculations suggest that the substructures of Bi⁺ in the sodalite cages contribute to the ultrabroad near-infrared emission. These results not only enrich the well-established spectrum of optically active zeolites and deepen the understanding of bismuth related photophysical behaviors, but also may raise new possibilities for the design and synthesis of novel hybrid nanoporous photonic materials activated by other heavier p-block elements

Biseokeaniamides A, B, and C, Sterol <i>O</i>‑Acyltransferase Inhibitors from an <i>Okeania</i> sp. Marine Cyanobacterium

Biseokeaniamides A, B, and C (<b>1</b>–<b>3</b>), structurally novel sterol <i>O</i>-acyltransferase (SOAT) inhibitors, were isolated from an <i>Okeania</i> sp. marine cyanobacterium. Their structures were elucidated by spectroscopic analyses and degradation reactions. Biseokeaniamide B (<b>2</b>) exhibited moderate cytotoxicity against human HeLa cancer cells, and compounds <b>1</b>–<b>3</b> inhibited both SOAT1 and SOAT2, not only at an enzyme level but also at a cellular level. Biseokeaniamides (<b>1</b>–<b>3</b>) are the first linear lipopeptides that have been shown to exhibit SOAT-inhibitory activity

K-Rta Wt but not Ring-finger domain mutant can degrade SUMO-modified proteins.

<p>(<b>A</b>) Flag-SUMO and K-Rta wild type or mutant were cotransfected into 293T cells, and probed with indicated antibodies. The K-Rta Ring-like domain (C141, H145) is important for SUMO degradation. (<b>B</b>) MG132 recovered SUMO proteins from degradation. 24 hours after the K-Rta transfection, MG132 or DMSO (vehicle) was added into the culture media and cells were harvested after 12 hours of treatment. SUMO-modified proteins were probed with anti-Flag antibody. (<b>C</b>) SUMO degradation during KSHV reactivation in BCBL-1. After induction of K-Rta expression in TREx-K-Rta-BCBL-1 with doxycycline (Dox), SUMO-modified proteins were probed with anti-Flag antibody. K-Rta induction was confirmed with an anti-K-Rta antibody and GAPDH was served as the loading control. (<b>D</b>) Recovery of SUMO-modified proteins with MG132 in BCBL-1. KSHV reactivation was triggered by induction of K-Rta in BCBL-1 cells in either the presence or absence of MG132. The amount of SUMO-modified proteins was examined by immunoblotting with an anti-Flag antibody. The accumulation of SUMO-modified conjugates was evident by increments of higher molecular weight entities.</p

STUbL-like function is important for K-Rta transactivation activity.

<p>Reporter assays were performed in 293 cells using the indicated K-Rta target gene reporters. Reporter plasmids were cotransfected with K-Rta Wt or mutants, and luciferase activity was measured at 48 hours post-transfection. Luciferase activity of reporter with empty expression plasmids was normalized to a value of 1. Fold activation over control is shown.</p

K-Rta degrades SUMO(+)K-bZIP but not SUMO(−)K-bZIP.

<p>K-Rta was cotransfected with the indicated K-bZIP plasmid and immunoblotting was performed with anti-K-bZIP antibody. Proteasome (MG132, MG; Epoxomicin, Epox) or lysosome inhibitors (chloroquine, Chlor) were added to the culture media after 24 hours transfection and incubated another 12 hours.</p

SUMO-degradation function is important for KSHV replication.

<p><b>(A)</b> Recombinant KSHV, which harbors a point mutation in the Ring domain of K-Rta or SIM domain was constructed and transfected into 293T cells. LANA expression was examined by RT-qPCR (a). Values are normalized to cellular GAPDH. Recombinant KSHV containing a K-Rta point mutation or revertant wild type virus was reactivated with combination of sodium butyrate (SB, 1 mM) and TPA (20 nM). Expression of K-Rta protein was confirmed by immunoblotting (b), and K-Rta target gene expression was examined by RT-qPCR (c). Values are normalized to cellular β-actin, and fold induction over latent cell is shown. <b>(B)</b> Viral replication. Recombinant KSHV replication was measured after reactivation with TPA, sodium butyrate, or combination of K-Rta expression and TPA treatment. KSHV encapsidated (DNase resistant) DNA copy number in the supernatant was measured by qt-PCR. Absolute viral copy number in 1 mL of supernatant is shown. K-Rta Wt but not mutant expression rescued viral replication.</p

Immunofluorescence analysis (IFA).

<p><b> (A)</b> IFA was performed with anti-PML (Green) and anti-K-Rta (Red) antibodies. Arrows indicate cells showing overexpression of K-Rta. <b>(B)</b> K-Rta degrades PML. PML wild type or PML del-SUMO mutant was cotransfected with K-Rta or K-Rta mutants. K-Rta wild type preferentially degrades PML wild type, which can be modified by SUMO in vivo. K-Rta Ring mutant (H145L) or SUMO-binding mutant (<i>Δ</i>SIM) was not able to degrade PML. <b>(C)</b> Endogenous SUMO-modified proteins. K-Rta expression was induced by addition of doxycycline (Dox). Cell lysates were prepared 48 hours post-induction. Indicated proteins were probed with specific antibodies and 25 µg of total protein was loaded in each lane. GAPDH was used as a loading control.</p

Degradation of SUMO by K-Rta.

<p>Plasmids expressing E1 (Uba2/Aos), E2 (Ubc9), SUMO-2, K-Rta or empty vector (Vec) were transfected into 293T cells. SUMO, K-Rta or tubulin was probed with respective antibody. <b>(A)</b> K-Rta reduced total SUMO-modified protein levels in a dose-dependent manner. <b>(B)</b> Overexpression of SUMO but not other SUMO enzymes recover the cellular SUMO-modified proteins.</p