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Identification of nucleolus localization signal of betanodavirus GGNNV protein α
Betanodavirus greasy grouper (Epinephelus tauvina) nervous necrosis viruses (GGNNV) protein α, a virus capsid protein, was detected in both nucleolus and cytoplasm of infected cells of Asian sea bass (SB) and transfected cells of SB and Cos-7 with pcDNA3.1/RNA2. To study its subcellular localization...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Science (USA).
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7126641/ https://www.ncbi.nlm.nih.gov/pubmed/12642096 http://dx.doi.org/10.1016/S0042-6822(02)00081-8 |
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author | Guo, Yan Xiang Dallmann, Klara Kwang, Jimmy |
author_facet | Guo, Yan Xiang Dallmann, Klara Kwang, Jimmy |
author_sort | Guo, Yan Xiang |
collection | PubMed |
description | Betanodavirus greasy grouper (Epinephelus tauvina) nervous necrosis viruses (GGNNV) protein α, a virus capsid protein, was detected in both nucleolus and cytoplasm of infected cells of Asian sea bass (SB) and transfected cells of SB and Cos-7 with pcDNA3.1/RNA2. To study its subcellular localization, ORF of protein α with 338 aa was fused with enhanced green fluorescent protein (EGFP) gene and was detected in transfected cells in the absence of other viral proteins. In both SB and Cos-7 cells, protein α was found to localize EGFP to the nucleolus and cytoplasm. Deletion mutants of protein α indicated that N-terminal 43 amino acid residues were required to import EGFP-α protein into the nucleolus. Further deletions within the 43 amino acid backbone, EGFP/33aa(1–33) and EGFP/30aa(14–43), localized to the nucleolus, suggesting that the 20 amino acids from 14 to 33 of protein α were the domain of nucleolus localization. To further determine the nucleolus targeting sequence, deletion mutations within the 20 amino acids of protein α were constructed. It was found that the deletion of (23)RRR(25), (29)RRR(31), or (23)RRRANNRRR(31) prevented the accumulation of EGFP fusion proteins into the nucleolus, demonstrating that (23)RRRANNRRR(31) contain the signal required for nucleolar localization. A similar distribution pattern of localization of protein α and its deletion mutants in SB and Cos-7 cells suggested that N-terminal residues of protein α (23)RRRANNRRR(31) constitute a nucleolus localization signal that functions in both fish and mammalian cells. |
format | Online Article Text |
id | pubmed-7126641 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | Elsevier Science (USA). |
record_format | MEDLINE/PubMed |
spelling | pubmed-71266412020-04-08 Identification of nucleolus localization signal of betanodavirus GGNNV protein α Guo, Yan Xiang Dallmann, Klara Kwang, Jimmy Virology Regular Article Betanodavirus greasy grouper (Epinephelus tauvina) nervous necrosis viruses (GGNNV) protein α, a virus capsid protein, was detected in both nucleolus and cytoplasm of infected cells of Asian sea bass (SB) and transfected cells of SB and Cos-7 with pcDNA3.1/RNA2. To study its subcellular localization, ORF of protein α with 338 aa was fused with enhanced green fluorescent protein (EGFP) gene and was detected in transfected cells in the absence of other viral proteins. In both SB and Cos-7 cells, protein α was found to localize EGFP to the nucleolus and cytoplasm. Deletion mutants of protein α indicated that N-terminal 43 amino acid residues were required to import EGFP-α protein into the nucleolus. Further deletions within the 43 amino acid backbone, EGFP/33aa(1–33) and EGFP/30aa(14–43), localized to the nucleolus, suggesting that the 20 amino acids from 14 to 33 of protein α were the domain of nucleolus localization. To further determine the nucleolus targeting sequence, deletion mutations within the 20 amino acids of protein α were constructed. It was found that the deletion of (23)RRR(25), (29)RRR(31), or (23)RRRANNRRR(31) prevented the accumulation of EGFP fusion proteins into the nucleolus, demonstrating that (23)RRRANNRRR(31) contain the signal required for nucleolar localization. A similar distribution pattern of localization of protein α and its deletion mutants in SB and Cos-7 cells suggested that N-terminal residues of protein α (23)RRRANNRRR(31) constitute a nucleolus localization signal that functions in both fish and mammalian cells. Elsevier Science (USA). 2003-02-15 2003-02-21 /pmc/articles/PMC7126641/ /pubmed/12642096 http://dx.doi.org/10.1016/S0042-6822(02)00081-8 Text en Copyright © 2003 Elsevier Science (USA). All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Regular Article Guo, Yan Xiang Dallmann, Klara Kwang, Jimmy Identification of nucleolus localization signal of betanodavirus GGNNV protein α |
title | Identification of nucleolus localization signal of betanodavirus GGNNV protein α |
title_full | Identification of nucleolus localization signal of betanodavirus GGNNV protein α |
title_fullStr | Identification of nucleolus localization signal of betanodavirus GGNNV protein α |
title_full_unstemmed | Identification of nucleolus localization signal of betanodavirus GGNNV protein α |
title_short | Identification of nucleolus localization signal of betanodavirus GGNNV protein α |
title_sort | identification of nucleolus localization signal of betanodavirus ggnnv protein α |
topic | Regular Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7126641/ https://www.ncbi.nlm.nih.gov/pubmed/12642096 http://dx.doi.org/10.1016/S0042-6822(02)00081-8 |
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