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Principles of protein targeting to the nucleolus

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dc.contributor.authorMartin, Robert M.
dc.contributor.authorTer-Avetisyan, Gohar
dc.contributor.authorHerce, Henry D.
dc.contributor.authorLudwig, Anne K.
dc.contributor.authorLättig-Tünnemann, Gisela
dc.contributor.authorCardoso, M. Cristina
dc.date.accessioned2021-07-20T11:11:40Z
dc.date.available2021-07-20T11:11:40Z
dc.date.issued2015
dc.description© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC© Robert M Martin, Gohar Ter-Avetisyan, Henry D Herce, Anne K Ludwig, Gisela Lättig-Tünnemann, and M Cristina Cardoso This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.pt_PT
dc.description.abstractThe nucleolus is the hallmark of nuclear compartmentalization and has been shown to exert multiple roles in cellular metabolism besides its main function as the place of rRNA synthesis and assembly of ribosomes. Nucleolar proteins dynamically localize and accumulate in this nuclear compartment relative to the surrounding nucleoplasm. In this study, we have assessed the molecular requirements that are necessary and sufficient for the localization and accumulation of peptides and proteins inside the nucleoli of living cells. The data showed that positively charged peptide entities composed of arginines alone and with an isoelectric point at and above 12.6 are necessary and sufficient for mediating significant nucleolar accumulation. A threshold of 6 arginines is necessary for peptides to accumulate in nucleoli, but already 4 arginines are sufficient when fused within 15 amino acid residues of a nuclear localization signal of a protein. Using a pH sensitive dye, we found that the nucleolar compartment is particularly acidic when compared to the surrounding nucleoplasm and, hence, provides the ideal electrochemical environment to bind poly-arginine containing proteins. In fact, we found that oligo-arginine peptides and GFP fusions bind RNA in vitro. Consistent with RNA being the main binding partner for arginines in the nucleolus, we found that the same principles apply to cells from insects to man, indicating that this mechanism is highly conserved throughout evolution.pt_PT
dc.description.sponsorshipRMM was supported by a post-doctoral grant from Fundação para a Ciência e Tecnologia, Portugal (SFRH-BPD-66611–2009). This work was supported by grants of the German Research Council (DFG CA198/3) to MCC.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationNucleus. 2015;6(4):314-325pt_PT
dc.identifier.doi10.1080/19491034.2015.1079680pt_PT
dc.identifier.eissn1949-1042
dc.identifier.issn949-1034
dc.identifier.urihttp://hdl.handle.net/10451/49023
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherInforma UKpt_PT
dc.relationSFRH-BPD-66611–2009pt_PT
dc.relation.publisherversionhttps://www.tandfonline.com/toc/kncl20/currentpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/pt_PT
dc.subjectGFPpt_PT
dc.subjectFluorescence microscopypt_PT
dc.subjectNucleolar localization sequencept_PT
dc.subjectNucleoluspt_PT
dc.subjectProtein targetingpt_PT
dc.titlePrinciples of protein targeting to the nucleoluspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage325pt_PT
oaire.citation.issue4pt_PT
oaire.citation.startPage314pt_PT
oaire.citation.titleNucleuspt_PT
oaire.citation.volume6pt_PT
person.familyNameMartin
person.givenNameRobert Manfred
person.identifier.ciencia-id7516-6C51-460B
person.identifier.orcid0000-0001-5600-7525
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublicationd50e7a9a-5216-4738-a5c6-94c8c0b85a1d
relation.isAuthorOfPublication.latestForDiscoveryd50e7a9a-5216-4738-a5c6-94c8c0b85a1d

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