Principles of protein targeting to the nucleolus

Detalhes bibliográficos
Autor(a) principal: Martin, Robert M.
Data de Publicação: 2015
Outros Autores: Ter-Avetisyan, Gohar, Herce, Henry D., Ludwig, Anne K., Lättig-Tünnemann, Gisela, Cardoso, M. Cristina
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/49023
Resumo: © 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.
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spelling Principles of protein targeting to the nucleolusGFPFluorescence microscopyNucleolar localization sequenceNucleolusProtein targeting© 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.The 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.RMM 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.Informa UKRepositório da Universidade de LisboaMartin, Robert M.Ter-Avetisyan, GoharHerce, Henry D.Ludwig, Anne K.Lättig-Tünnemann, GiselaCardoso, M. Cristina2021-07-20T11:11:40Z20152015-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/49023engNucleus. 2015;6(4):314-325949-103410.1080/19491034.2015.10796801949-1042info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T16:52:14Zoai:repositorio.ul.pt:10451/49023Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T22:00:33.796557Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Principles of protein targeting to the nucleolus
title Principles of protein targeting to the nucleolus
spellingShingle Principles of protein targeting to the nucleolus
Martin, Robert M.
GFP
Fluorescence microscopy
Nucleolar localization sequence
Nucleolus
Protein targeting
title_short Principles of protein targeting to the nucleolus
title_full Principles of protein targeting to the nucleolus
title_fullStr Principles of protein targeting to the nucleolus
title_full_unstemmed Principles of protein targeting to the nucleolus
title_sort Principles of protein targeting to the nucleolus
author Martin, Robert M.
author_facet Martin, Robert M.
Ter-Avetisyan, Gohar
Herce, Henry D.
Ludwig, Anne K.
Lättig-Tünnemann, Gisela
Cardoso, M. Cristina
author_role author
author2 Ter-Avetisyan, Gohar
Herce, Henry D.
Ludwig, Anne K.
Lättig-Tünnemann, Gisela
Cardoso, M. Cristina
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Martin, Robert M.
Ter-Avetisyan, Gohar
Herce, Henry D.
Ludwig, Anne K.
Lättig-Tünnemann, Gisela
Cardoso, M. Cristina
dc.subject.por.fl_str_mv GFP
Fluorescence microscopy
Nucleolar localization sequence
Nucleolus
Protein targeting
topic GFP
Fluorescence microscopy
Nucleolar localization sequence
Nucleolus
Protein targeting
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.
publishDate 2015
dc.date.none.fl_str_mv 2015
2015-01-01T00:00:00Z
2021-07-20T11:11:40Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10451/49023
url http://hdl.handle.net/10451/49023
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Nucleus. 2015;6(4):314-325
949-1034
10.1080/19491034.2015.1079680
1949-1042
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Informa UK
publisher.none.fl_str_mv Informa UK
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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