The behaviour of Nautilus pompilius swimming freely in a controlled mesocosm (tower tank, 4 m diameter x 10.5 m deep) was monitored using ultrasonic depth telemetry. Initially depths were monitored in water equilibrated with air. Then the bottom 3.5 m were rendered hypoxic (Po(2) <20 mmHg) and depths monitored again. A thermocline at 7-m depth (17 degrees C below, 20 degrees C above) prevented mixing with the top, normoxic water. Mean depth was significantly greater during the light phase (8.9 m) of the 12L : 12D photoperiod than the dark phase (5.6 m), but this was not affected by hypoxia. During the light phase animals preferred the bottom 2.5 m of the tank but showed no specific preference for any depth range during the dark phase. Hypoxia did not alter these patterns of depth preference, though one animal made regular excursions toward normoxic water during the light phase. Vertical swimming activity was almost twofold greater during the dark phase and was not affected by hypoxia. These data suggest that, at least over the short term, Nautilus are not constrained from entering areas with low dissolved oxygen. This hypoxia tolerance may be attributed to the large onboard oxygen stores and suppressed metabolism during hypoxia.
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http://dx.doi.org/10.1086/376428 | DOI Listing |
Int J Mol Sci
December 2022
Departament de Genètica, Microbiologia i Estadística, Facultat de Biologia, Universitat de Barcelona, E-08028 Barcelona, Spain.
Protein domains are independent structural and functional modules that can rearrange to create new proteins. While the evolution of multidomain proteins through the shuffling of different preexisting domains has been well documented, the evolution of domain repeat proteins and the origin of new domains are less understood. Metallothioneins (MTs) provide a good case study considering that they consist of metal-binding domain repeats, some of them with a likely de novo origin.
View Article and Find Full Text PDFPLoS One
July 2022
N°34, rue Thomy Célières, Nouméa, New Caledonia.
Modern nautilids (Nautilus and Allonautilus) have often been studied by paleontologists to better understand the anatomy and ecology of fossil relatives. Because direct observations of these animals are difficult, the analysis of light stable isotopes (C, O) preserved in their shells has been employed to reveal their habitat and life history. We aim to (1) reconstruct the habitat depth of Nautilus macromphalus and (2) decipher the fraction of metabolic carbon in its shell by analyzing oxygen and carbon isotopes (δ18O, δ13C) in the septa of two specimens in combination with analyses of water samples from the area.
View Article and Find Full Text PDFMar Drugs
July 2022
Zhejiang Key Laboratory of Aquatic Germplasm Resources, College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, China.
Hemocyanins present in the hemolymph of invertebrates are multifunctional proteins that are responsible for oxygen transport and play crucial roles in the immune system. They have also been identified as a source of antimicrobial peptides during infection in mollusks. Hemocyanin has also been identified in the cephalopod ancestor Nautilus, but antimicrobial peptides derived from the hemocyanin of have not been reported.
View Article and Find Full Text PDFJ R Soc Interface
June 2022
B CUBE - Center for Molecular Bioengineering, Technische Universität Dresden, Dresden, Germany.
The ability of evolution to shape organic form involves the interactions of multiple systems of constraints, including fabrication, phylogeny and function. The tendency to place function above everything else has characterized some of the historical biological literature as a series of 'Just-So' stories that provided untested explanations for individual features of an organism. A similar tendency occurs in biomaterials research, where features for which a mechanical function can be postulated are treated as an adaptation.
View Article and Find Full Text PDFGenes (Basel)
November 2021
Graduate School of Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Despite being a member of the shelled mollusks (Conchiferans), most members of extant cephalopods have lost their external biomineralized shells, except for the basally diverging Nautilids. Here, we report the result of our study to identify major Shell Matrix Proteins and their domains in the Nautilid in order to gain a general insight into the evolution of Conchiferan Shell Matrix Proteins. In order to do so, we performed a multiomics study on the shell of , by conducting transcriptomics of its mantle tissue and proteomics of its shell matrix.
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