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Autoren: Schäfer, Gabriela Giannina
Grebe, Lukas Jörg
Depoix, Frank
Lieb, Bernhard
Titel: Hemocyanins of Muricidae : New ‘Insights’ Unravel an Additional Highly Hydrophilic 800 kDa Mass Within the Molecule
Online-Publikationsdatum: 28-Jun-2022
Erscheinungsdatum: 2021
Sprache des Dokuments: Englisch
Zusammenfassung/Abstract: Hemocyanins are giant oxygen transport proteins that freely float within the hemolymph of most molluscs. The basic quaternary structure of molluscan hemocyanins is a cylindrical decamer with a diameter of 35 nm which is built of 400 kDa subunits. Previously published results, however, showed that one out of two hemocyanin subunits of Rapana venosa encompasses two polypeptides, one 300 kDa and one 100 kDa polypeptide which aggregate to typical 4 MDa and 8 MDa hemocyanin (di-)decamer molecules. It was shown that the polypeptides are bound most probably by one or more cysteine disulfide bridges but it remained open if these polypeptides were coded by one or two genes. Our here presented results clearly showed that both polypeptides are coded by one gene only and that this phenomenon can also be found in the gastropod Nucella lapillus. Thus, it can be defined as clade-specific for Muricidae, a group of the very diverse Caenogastropoda. In addition, we discovered a further deviation of this hemocyanin subunit within both species, namely a region of 340 mainly hydrophilic amino acids (especially histidines and aspartic acids) which have not been identified in any other molluscan hemocyanin, yet. Our results indicate that, within the quaternary structure, these additional amino acids most probably protrude within the inner part of didecamer cylinders, forming a large extra mass of up to 800 kDa. They presumably influence the structure of the protein and may affect the functionality. Thus, these findings reveal further insights into the evolution and structures of gastropod hemocyanins.
DDC-Sachgruppe: 570 Biowissenschaften
570 Life sciences
Veröffentlichende Institution: Johannes Gutenberg-Universität Mainz
Organisationseinheit: FB 10 Biologie
Veröffentlichungsort: Mainz
Version: Published version
Publikationstyp: Zeitschriftenaufsatz
Nutzungsrechte: CC BY
Informationen zu den Nutzungsrechten:
Zeitschrift: Journal of molecular evolution
Seitenzahl oder Artikelnummer: 62
Verlag: Springer
Verlagsort: New York, NY
Erscheinungsdatum: 2021
ISSN: 1432-1432
DOI der Originalveröffentlichung: 10.1007/s00239-020-09986-6
Enthalten in den Sammlungen:JGU-Publikationen

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