Wege, M. | Search bioRxiv

bioRxiv2025

Shedding dynamics of the Ross seal (Ommatophoca rossii) whiskers investigated through carbon and nitrogen bulk stable isotope composition

Understanding the trophic ecology of pinnipeds is essential to define their role in ecosystems and anticipate their responses as top predators to environmental changes. Incremental analyses of carbon ({delta}13C) and nitrogen ({delta}15N) stable isotopes along their whiskers provide valuable records of their foraging habitat and trophic level over time. The effectiveness of this approach relies on knowledge of species-specific whisker shedding dynamics and growth rates. We investigated the shedding dynamics of Ross seal (Ommatophoca rossii) whiskers and attempted to evaluate the time captured in these tissues by combining whiskers bulk{delta} 13C and{delta} 15N incremental measurements with satellite tracking data, collected after whisker growth. Our tracking data are consistent with previous studies, in that Ross seals migrate post-moult between the marginal ice zone and the Antarctic Polar Front. Stable isotope profiles of whiskers did not show the typical decrease in{delta} {superscript 1}3C and increase in{delta} {superscript 1}N values at the whiskers tip that would be expected if shedding coincided with the annual fur moult, when fasting typically occurs. The occurrence of similar isotope variations, which were offset between the left and right whiskers of the same individual in relation to distance from the muzzle, further suggest asynchronous, non-seasonal whisker shedding. Our inability to identify known cyclic phenological events (i.e., fasting periods or seasonal migrations) prevented the determination of the average growth rate of whiskers. The additional data on whisker shedding dynamics of Ross seals is a valuable first step in support of future ecological studies based on the whiskers of this species.

ecology↗

bioRxiv2021

Comparative analysis of bile-salt degradation in Sphingobium sp. strain Chol11 and P. stutzeri Chol1 reveals functional diversity of β-proteobacterial steroid degradation enzymes and suggests a novel reaction sequence for side-chain degradation involving a hydroxylation step

The reaction sequence for aerobic degradation of bile salts by environmental bacteria resembles degradation of other steroid compounds. Recent findings show that bacteria belonging to the Sphingomonadaceae use a pathway variant for bile-salt degradation. This study addresses this so-called {Delta}4,6 -variant by comparative analysis of unknown degradation steps in Sphingobium sp. strain Chol11 with known reactions found in Pseudomonas stutzeri Chol1. Investigations with strain Chol11 revealed an essential function of the acyl-CoA dehydrogenase Scd4AB for growth with bile salts. Growth of the scd4AB deletion mutant was restored with a metabolite containing a double bond within the side chain which was produced by the {Delta}22-acyl-CoA dehydrogenase Scd1AB from P. stutzeri Chol1. Expression of scd1AB in the scd4AB deletion mutant fully restored growth with bile salts while expression of scd4AB only enabled constricted growth in P. stutzeri Chol1 scd1A or scd1B deletion mutants. Strain Chol11 {Delta}scd4A accumulated hydroxylated steroid metabolites which were degraded and activated with coenzyme A by the wild type. Activities of five Rieske type monooxygenases of strain Chol11 were screened by heterologous expression and compared to the B-ring cleaving KshABChol1 from P. stutzeri Chol1. Three of the Chol11 enzymes catalyzed B-ring cleavage of only {Delta}4,6 -steroids while KshABChol1 was more versatile. Expression of a fourth KshA homolog, Nov2c228 led to production of metabolites with hydroxylations at an unknown position. These results indicate functional diversity of {beta}-proteobacterial enzymes for bile-salt degradation and suggest a novel side-chain degradation pathway involving an essential ACAD reaction and a steroid hydroxylation step. ImportanceThis study highlights the biochemical diversity of bacterial degradation of steroid compounds in different aspects. First, it further elucidates an unexplored variant in the degradation of bile-salt side chains by Sphingomonads, a group of environmental bacteria that is well-known for their broad metabolic capabilities. Moreover, it adds a so-far unknown hydroxylation of steroids to the reactions Rieske monooxygenases can catalyze with steroids. Additionally, it analyzes the first proteobacterial ketosteroid-9-hydroxylase and shows that this enzyme is able to catalyze side reactions with non-native substrates.

microbiology↗