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      Characterization of the Fishing Lines in Titiwai (= Arachnocampa luminosa Skuse, 1890) from New Zealand and Australia

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          Abstract

          Animals use adhesive secretions in a plethora of ways, either for attachment, egg anchorage, mating or as either active or passive defence. The most interesting function, however, is the use of adhesive threads to capture prey, as the bonding must be performed within milliseconds and under unsuitable conditions (movement of prey, variable environmental conditions, unfavourable attack angle, etc.) to be nonetheless successful. In the following study a detailed characterization of the prey capture system of the world-renowned glowworm group Arachnocampa from the macroscopic to the ultrastructural level is performed. The data reveal that the adhesive droplets consist mostly of water and display hygroscopic properties at varying humidity levels. The droplet core of Arachnocampa luminosa includes a certain amount of the elements sodium, sulphur and potassium (beside carbon, oxygen and nitrogen), while a different element composition is found in the two related species A. richardsae and A. tasmaniensis. Evidence for lipids, carbohydrates and proteins was negative on the histochemical level, however X-ray photoelectron spectroscopy confirm the presence of peptides within the droplet content. Different to earlier assumptions, the present study indicates that rather than oxalic acid, urea or uric acid are present in the adhesive droplets, presumably originating from the gut. Comparing the capture system in Arachnocampa with those of orb-spiders, large differences appear not only regarding the silky threads, but also, in the composition, hygroscopic properties and size of the mucous droplets.

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          Most cited references30

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          Evolution of arthropod silks.

          Silks belong to the class of molecules called structural proteins. The ability to produce silk proteins has evolved multiple times in the arthropods, and silk secreting glands have evolved via two different pathways. The comparative data and phylogenetic analyses in this review suggest that the silk-secreting systems of spiders and insects are homologous and linked to the crural gland (origin of systemic pathway to silk production) and cuticular secretions (origin of surficial pathway to silk production) of an onychophoran-like ancestor. The evolution of silk secreting organs via a surficial pathway is possible in adult and larval hexapods, regardless of their developmental mode. Silk secretion via a systemic pathway is possible in either adult or larval hexapods, but only larval insects have dedicated silk producing glands. Spiders, however, have evolved silk producing systems via both systemic pathway and surficial pathways, and a single individual retains both throughout its lifespan. Early in the evolution of spiders, silk glands were undifferentiated, suggesting that the number of silk secreting glands of any individual was related to the spider's energetic need to produce large quantities of protein. However, the complex silk-producing systems that characterize the aerial web-building spiders and the diverse types of proteins they produce suggest that their silks reflect the diverse and increasing number of ways in which spiders use them. Because the muscular and innervated spinnerets and spigots of spiders allow them to control fiber functional properties, silk proteins represent an avenue through which animal behavior may directly affect the molecular properties of a protein.
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            Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes.

            Firefly luciferase is a 62 kDa protein that catalyzes the production of light. In the presence of MgATP and molecular oxygen, the enzyme oxidizes its substrate, firefly luciferin, emitting yellow-green light. The reaction proceeds through activation of the substrate to form an adenylate intermediate. Firefly luciferase shows extensive sequence homology with a number of enzymes that utilize ATP in adenylation reactions. We have determined the crystal structure of firefly luciferase at 2.0 A resolution. The protein is folded into two compact domains. The large N-terminal domain consists of a beta-barrel and two beta-sheets. The sheets are flanked by alpha-helices to form an alphabetaalphabetaalpha five-layered structure. The C-terminal portion of the molecule forms a distinct domain, which is separated from the N-terminal domain by a wide cleft. Firefly luciferase is the first member of a superfamily of homologous enzymes, which includes acyl-coenzyme A ligases and peptide synthetases, to have its structure characterized. The residues conserved within the superfamily are located on the surfaces of the two domains on either side of the cleft, but are too far apart to interact simultaneously with the substrates. This suggests that the two domains will close in the course of the reaction. Firefly luciferase has a novel structural framework for catalyzing adenylate-forming reactions.
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              Spider web glue: two proteins expressed from opposite strands of the same DNA sequence.

              The various silks that make up the web of the orb web spiders have been studied extensively. However, success in prey capture depends as much on the web glue as on the fibers. Spider silk glue, which is considered one of the strongest and most effective biological glues, is an aqueous solution secreted from the orb weaving spider's aggregate glands and coats the spiral prey capturing threads of their webs. Studies identified the major component of the glue as microscopic nodules made of a glycoprotein. This study describes two newly discovered proteins that form the glue-glycoprotein of the golden orb weaving spider Nephila clavipes . Our results demonstrate that both proteins contain unique 110 amino acid repetitive domains that are encoded by opposite strands of the same DNA sequence. Thus, the genome of the spider encodes two distinct yet functionally related genes by using both strands of an identical DNA sequence. Moreover, the closest match for the nonrepetitive region of one of the proteins is chitin binding proteins. The web glue appears to have evolved a substantial level of sophistication matching that of the spider silk fibers.
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                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                PLoS ONE
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, CA USA )
                1932-6203
                14 December 2016
                2016
                : 11
                : 12
                : e0162687
                Affiliations
                [1 ]Ludwig Boltzmann Institute for Experimental and Clinical Traumatology, Vienna, Austria
                [2 ]University of Vienna, Faculty of Life Science, Core Facility Cell Imaging & Ultrastructure Research, Vienna, Austria
                [3 ]Technical University Wien, Institute of Chemical Technologies and Analytics, Vienna, Austria
                [4 ]The University of Queensland, School of Biological Sciences, Brisbane, Queensland, Australia
                [5 ]Spellbound Cave, Waitomo, New Zealand
                [6 ]Department of Conservation, Wellington, New Zealand
                [7 ]University of Otago, School of Medical Sciences, Department of Anatomy, Otago Centre for Confocal Microscopy, Otago, New Zealand
                [8 ]Fraunhofer Institute for Manufacturing Technology and Advanced Materials, Department of Adhesive Bonding Technology and Surfaces, Bremen, Germany
                Swedish University of Agricultural Sciences, SWEDEN
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                • Conceptualization: JvB IS PC.

                • Data curation: JvB.

                • Formal analysis: VD MMD NC IS AM KT MN.

                • Funding acquisition: JvB.

                • Investigation: JvB.

                • Methodology: JvB IS PC VD.

                • Project administration: JvB.

                • Resources: JvB PC IG MMD MN KT.

                • Writing – original draft: JvB.

                • Writing – review & editing: VD MMD DJM IS IG.

                Author information
                http://orcid.org/0000-0001-7243-0438
                Article
                PONE-D-16-12012
                10.1371/journal.pone.0162687
                5156358
                27973586
                b79b84cd-ae8e-4a87-b8d8-11143613de30
                © 2016 von Byern et al

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

                History
                : 23 March 2016
                : 27 August 2016
                Page count
                Figures: 12, Tables: 5, Pages: 30
                Funding
                Funded by: funder-id http://dx.doi.org/10.13039/501100002428, Austrian Science Fund;
                Award ID: 24531-B17
                Award Recipient :
                This work was supported by the Austrian Science Foundation FWF (Project No. AP 24531-B17).
                Categories
                Research Article
                Physical Sciences
                Materials Science
                Materials by Structure
                Crystals
                Physical Sciences
                Chemistry
                Chemical Compounds
                Organic Compounds
                Urea
                Physical Sciences
                Chemistry
                Organic Chemistry
                Organic Compounds
                Urea
                Physical Sciences
                Materials Science
                Materials by Attribute
                Adhesives
                Biology and Life Sciences
                Developmental Biology
                Life Cycles
                Larvae
                Earth Sciences
                Atmospheric Science
                Meteorology
                Humidity
                Physical Sciences
                Chemistry
                Chemical Compounds
                Acids
                Uric Acid
                Research and Analysis Methods
                Microscopy
                Light Microscopy
                Polarized Light Microscopy
                Physical Sciences
                Chemistry
                Chemical Elements
                Carbon
                Custom metadata
                Data are available from Figshare (DOI: https://dx.doi.org/10.6084/m9.figshare.3492518; URL: https://figshare.com/s/e63cf915842964c9bf0b).

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