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Biology subjects

Maloney, M. E.

Publications and source records attributed to Maloney, M. E..

2 recordsLinked to original sources

Blue appendages and temperature acclimation increase survival during acute heat stress in the upside-down jellyfish, Cassiopea xamachana

Upside-down jellyfish (Cassiopea sp.) are highly tolerant to multiple abiotic stressors, including fluctuating temperatures associated with shallow marine habitats. This resilience may underlie the ability of Cassiopea sp. to inhabit a wide variety of tropical habitats across the globe. Additionally, Cassiopea sp. are marked by a conspicuous array of appendage coloration; individual medusae vary in the hue and number of oral appendages, which are often strikingly blue. The function of this coloration is not understood. We aimed to understand how extrinsic and intrinsic factors may shape thermal tolerance. Adult Cassiopea xamachana were collected from two sites that vary in daily temperature range within the Florida Keys and were subjected to acute lethal heat stress experiments. To quantify a whole-organism response to heat, we measured changes in bell pulsation, which likely plays a role in feeding, oxygen exchange, and symbiont uptake. Results show that C. xamachana from the two collection sites do not exhibit different responses to heat, suggesting that temperature fluctuations do not prime individuals for higher thermal tolerance. Additionally, C. xamachana with blue appendages survived significantly higher temperatures and exhibited less change in bell pulsation rates compared to non-blue individuals. Finally, color morphs were acclimated at either ambient (26 {degrees}C) or elevated (33 {degrees}C) temperatures. We found that acclimation at 33 {degrees}C, as well as appendage color in each treatment, led to higher survival under acute heat stress. Together, these findings highlight the importance of phenotypic plasticity and coloration in Cassiopea resilience during heat stress.

ecology↗

Discovery of the 1-naphthylamine biodegradation pathway reveals an enzyme that catalyzes 1-naphthylamine glutamylation

1-Naphthylamine (1NA), which is harmful to human and aquatic animals, has been used widely in the manufacturing of dyes, pesticides, and rubber antioxidants. Nevertheless, little is known about its environmental behavior and no bacteria have been reported to use it as the growth substrate. Herein, we describe a pathway for 1NA degradation in isolate Pseudomonas sp. strain JS3066, determine the structure and mechanism of the enzyme NpaA1 that catalyzes the initial reaction, and reveal how the pathway evolved. From genetic and enzymatic analysis, a cluster of 5 genes encoding a dioxygenase system was determined to be responsible for the initial steps in 1NA degradation through glutamylation of 1NA. The {gamma}-glutamylated 1NA was subsequently oxidized to 1,2-dihydroxynaphthalene which was further degraded by the well-established pathway of naphthalene degradation via catechol. Enzymatic analysis showed that NpaA1 catalyzed conversion of various anilines and naphthylamine derivatives. Structural and biochemical studies of NpaA1 revealed that the broad substrate specificity of NpaA1 is due to a large hydrophobic pocket, which is different from type I glutamine synthetase (GSI). The findings enhance understanding of degrading polycyclic aromatic amines, and will also enable the application of bioremediation at naphthylamine contaminated sites.

microbiology↗