Gutenberg Open Science: Hemocyanins of Muricidae : New ‘Insights’ Unravel an Additional Highly Hydrophilic 800 kDa Mass Within the Molecule

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-7238

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DC Field	Value	Language
dc.contributor.author	Schäfer, Gabriela Giannina	-
dc.contributor.author	Grebe, Lukas Jörg	-
dc.contributor.author	Depoix, Frank	-
dc.contributor.author	Lieb, Bernhard	-
dc.date.accessioned	2022-06-28T09:55:49Z	-
dc.date.available	2022-06-28T09:55:49Z	-
dc.date.issued	2021	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/7252	-
dc.description.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.	en_GB
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	570 Biowissenschaften	de_DE
dc.subject.ddc	570 Life sciences	en_GB
dc.title	Hemocyanins of Muricidae : New ‘Insights’ Unravel an Additional Highly Hydrophilic 800 kDa Mass Within the Molecule	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-7238	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 10 Biologie	de
jgu.organisation.number	7970	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Journal of molecular evolution	de
jgu.journal.volume	89	de
jgu.pages.start	62	de
jgu.pages.end	72	de
jgu.publisher.year	2021	-
jgu.publisher.name	Springer	de
jgu.publisher.place	New York, NY	de
jgu.publisher.issn	1432-1432	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	570	de
jgu.publisher.doi	10.1007/s00239-020-09986-6	de
jgu.organisation.ror	https://ror.org/023b0x485
Appears in collections:	JGU-Publikationen

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