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Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ

The newly developed oocyte shuttle protein contains a streptavidin moiety that tightly binds biotinylated DNA. Injected intravenously into adult Xenopus females, the protein-DNA complex is rapidly transported through the bloodstream and, within the ovary, the vitellogenin ligand present in the prote...

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Autores principales: Rungger, Duri, Muster, Lisbeth, Georgiev, Oleg, Rungger-Brändle, Elisabeth
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5312104/
https://www.ncbi.nlm.nih.gov/pubmed/28202471
http://dx.doi.org/10.1242/bio.022376
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author Rungger, Duri
Muster, Lisbeth
Georgiev, Oleg
Rungger-Brändle, Elisabeth
author_facet Rungger, Duri
Muster, Lisbeth
Georgiev, Oleg
Rungger-Brändle, Elisabeth
author_sort Rungger, Duri
collection PubMed
description The newly developed oocyte shuttle protein contains a streptavidin moiety that tightly binds biotinylated DNA. Injected intravenously into adult Xenopus females, the protein-DNA complex is rapidly transported through the bloodstream and, within the ovary, the vitellogenin ligand present in the protein binds to the receptors at the surface of the oocytes. The bound complex is internalized and translocates into the oocyte nucleus thanks to an SV40 nuclear localization signal, enhanced by an adjacent casein kinase phosphorylation site. Functioning of the shuttle protein is documented by transporting DNA molecules that, upon intramolecular homologous recombination within the oocyte nucleus, express easily traceable markers such as green fluorescence or tetracycline resistance.
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spelling pubmed-53121042017-03-06 Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ Rungger, Duri Muster, Lisbeth Georgiev, Oleg Rungger-Brändle, Elisabeth Biol Open Research Article The newly developed oocyte shuttle protein contains a streptavidin moiety that tightly binds biotinylated DNA. Injected intravenously into adult Xenopus females, the protein-DNA complex is rapidly transported through the bloodstream and, within the ovary, the vitellogenin ligand present in the protein binds to the receptors at the surface of the oocytes. The bound complex is internalized and translocates into the oocyte nucleus thanks to an SV40 nuclear localization signal, enhanced by an adjacent casein kinase phosphorylation site. Functioning of the shuttle protein is documented by transporting DNA molecules that, upon intramolecular homologous recombination within the oocyte nucleus, express easily traceable markers such as green fluorescence or tetracycline resistance. The Company of Biologists Ltd 2017-02-08 /pmc/articles/PMC5312104/ /pubmed/28202471 http://dx.doi.org/10.1242/bio.022376 Text en © 2017. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
spellingShingle Research Article
Rungger, Duri
Muster, Lisbeth
Georgiev, Oleg
Rungger-Brändle, Elisabeth
Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ
title Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ
title_full Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ
title_fullStr Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ
title_full_unstemmed Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ
title_short Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ
title_sort oocyte shuttle, a recombinant protein transporting donor dna into the xenopus oocyte in situ
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5312104/
https://www.ncbi.nlm.nih.gov/pubmed/28202471
http://dx.doi.org/10.1242/bio.022376
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