Nucleolar localization of c‐Jun

FEBS Journal ◽  
2021 ◽  
Author(s):  
Tetsuaki Miyake ◽  
John C. McDermott
Keyword(s):  
Nucleolar Localization

scholarly journals Mutation of the N-Terminal Region of Chikungunya Virus Capsid Protein: Implications for Vaccine Design

mBio ◽  
2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Adam Taylor ◽  
Xiang Liu ◽  
Ali Zaid ◽  
Lucas Y. H. Goh ◽  
Jody Hobson-Peters ◽  
...  
Keyword(s):  
Host Cell ◽  
Capsid Protein ◽  
Chikungunya Virus ◽  
Fluorescent Protein ◽  
Nuclear Translocation ◽  
Vaccine Design ◽  
Terminal Region ◽  
Site Directed Mutagenesis ◽  
Nucleolar Localization ◽  
Localization Sequence

ABSTRACTMosquito-transmitted chikungunya virus (CHIKV) is an arthritogenic alphavirus of theTogaviridaefamily responsible for frequent outbreaks of arthritic disease in humans. Capsid protein, a structural protein encoded by the CHIKV RNA genome, is able to translocate to the host cell nucleolus. In encephalitic alphaviruses, nuclear translocation induces host cell transcriptional shutoff; however, the role of capsid protein nucleolar localization in arthritogenic alphaviruses remains unclear. Using recombinant enhanced green fluorescent protein (EGFP)-tagged expression constructs and CHIKV infectious clones, we describe a nucleolar localization sequence (NoLS) in the N-terminal region of capsid protein, previously uncharacterized in CHIKV. Mutation of the NoLS by site-directed mutagenesis reduced efficiency of nuclear import of CHIKV capsid protein. In the virus, mutation of the capsid protein NoLS (CHIKV-NoLS) attenuated replication in mammalian and mosquito cells, producing a small-plaque phenotype. Attenuation of CHIKV-NoLS is likely due to disruption of the viral replication cycle downstream of viral RNA synthesis. In mice, CHIKV-NoLS infection caused no disease signs compared to wild-type CHIKV (CHIKV-WT)-infected mice; lack of disease signs correlated with significantly reduced viremia and decreased expression of proinflammatory factors. Mice immunized with CHIKV-NoLS, challenged with CHIKV-WT at 30 days postimmunization, develop no disease signs and no detectable viremia. Serum from CHIKV-NoLS-immunized mice is able to efficiently neutralize CHIKV infectionin vitro. Additionally, CHIKV-NoLS-immunized mice challenged with the related alphavirus Ross River virus showed reduced early and peak viremia postchallenge, indicating a cross-protective effect. The high degree of CHIKV-NoLS attenuation may improve CHIKV antiviral and rational vaccine design.IMPORTANCECHIKV is a mosquito-borne pathogen capable of causing explosive epidemics of incapacitating joint pain affecting millions of people. After a series of major outbreaks over the last 10 years, CHIKV and its mosquito vectors have been able to expand their range extensively, now making CHIKV a human pathogen of global importance. With no licensed vaccine or antiviral therapy for the treatment of CHIKV disease, there is a growing need to understand the molecular determinants of viral pathogenesis. These studies identify a previously uncharacterized nucleolar localization sequence (NoLS) in CHIKV capsid protein, begin a functional analysis of site-directed mutants of the capsid protein NoLS, and examine the effect of the NoLS mutation on CHIKV pathogenesisin vivoand its potential to influence CHIKV vaccine design. A better understanding of the pathobiology of CHIKV disease will aid the development of effective therapeutic strategies.

scholarly journals Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein B23.

1994 ◽  
Vol 269 (38) ◽  
pp. 23776-23783
Author(s):  
B.C. Valdez ◽  
L. Perlaky ◽  
D. Henning ◽  
Y. Saijo ◽  
P.K. Chan ◽  
...  
Keyword(s):  
Nucleolar Localization ◽  
Protein B23

Nucleolar localization of the RNA helicase DDX21 is associated with decreased survival in advanced-stage endometrioid endometrial cancer

2021 ◽  
Vol 162 ◽  
pp. S214
Author(s):  
Jessica Parker ◽  
Hao Chen ◽  
Jayanthi Lea ◽  
W. Lee Kraus
Keyword(s):  
Endometrial Cancer ◽  
Rna Helicase ◽  
Nucleolar Localization ◽  
Advanced Stage ◽  
Endometrioid Endometrial Cancer

scholarly journals Nuclear/nucleolar localization properties of C-terminal nucleocapsid protein of SARS coronavirus

2005 ◽  
Vol 114 (1-2) ◽  
pp. 23-34 ◽  
Author(s):  
Khalid Amine Timani ◽  
Qingjiao Liao ◽  
Linbai Ye ◽  
Yingchun Zeng ◽  
Jing Liu ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Nucleolar Localization ◽  
Sars Coronavirus

scholarly journals Mitotic Expression of Spo13 Alters M-Phase Progression and Nucleolar Localization of Cdc14 in Budding Yeast

Genetics ◽  
2010 ◽  
Vol 185 (3) ◽  
pp. 841-854 ◽  
Author(s):  
Elisa Varela ◽  
Ulrich Schlecht ◽  
Anca Moina ◽  
James D. Fackenthal ◽  
Brian K. Washburn ◽  
...  
Keyword(s):  
Budding Yeast ◽  
Nucleolar Localization ◽  
M Phase ◽  
Phase Progression

Sequence requirement for the nucleolar localization of human I-mfa domain-containing protein (HIC p40)

2000 ◽  
Vol 79 (11) ◽  
pp. 834-838 ◽  
Author(s):  
Sabine Thébault ◽  
Jihane Basbous ◽  
Bernard Gay ◽  
Christian Devaux ◽  
Jean-Michel Mesnard
Keyword(s):  
Nucleolar Localization

Nucleolar Localization/Retention Signals

2013 ◽  
pp. 175-196 ◽  
Author(s):  
Eugene V. Sheval ◽  
Yana R. Musinova
Keyword(s):  
Nucleolar Localization

scholarly journals Regions of bovine adenovirus-3 IVa2 involved in nuclear/nucleolar localization and interaction with pV

Virology ◽  
2020 ◽  
Vol 546 ◽  
pp. 25-37
Author(s):  
Tekeleselassie Woldemariam ◽  
Wenxiu Wang ◽  
Abdelrahman Said ◽  
Suresh K. Tikoo
Keyword(s):  
Nucleolar Localization ◽  
Bovine Adenovirus

Differential roles of two DDX17 isoforms in the formation of membraneless organelles

2020 ◽  
Vol 168 (1) ◽  
pp. 33-40
Author(s):  
Yuya Hirai ◽  
Eisuke Domae ◽  
Yoshihiro Yoshikawa ◽  
Keizo Tomonaga
Keyword(s):  
Amino Acid ◽  
Enzymatic Activity ◽  
Rna Helicase ◽  
Intracellular Distribution ◽  
Amino Acid Sequences ◽  
Nucleolar Localization ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Dead Box ◽  
Additional Amino Acid

Abstract The RNA helicase, DDX17 is a member of the DEAD-box protein family. DDX17 has two isoforms: p72 and p82. The p82 isoform has additional amino acid sequences called intrinsically disordered regions (IDRs), which are related to the formation of membraneless organelles (MLOs). Here, we reveal that p72 is mostly localized to the nucleoplasm, while p82 is localized to the nucleoplasm and nucleoli. Additionally, p82 exhibited slower intranuclear mobility than p72. Furthermore, the enzymatic mutants of both p72 and p82 accumulate into the stress granules. The enzymatic mutant of p82 abolishes nucleolar localization of p82. Our findings suggest the importance of IDRs and enzymatic activity of DEAD-box proteins in the intracellular distribution and formation of MLOs.

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