scholarly journals Identification and Characterization of a Functional Nuclear Localization Signal in the HIV-1 Integrase Interactor LEDGF/p75

2004 ◽  
Vol 279 (32) ◽  
pp. 33421-33429 ◽  
Author(s):  
Goedele Maertens ◽  
Peter Cherepanov ◽  
Zeger Debyser ◽  
Yves Engelborghs ◽  
Alan Engelman
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Localization Signal ◽  
Functional Nuclear Localization Signal ◽  
Identification And Characterization ◽  
Hiv 1

Identification and characterization of a nuclear localization signal of TRIM28 that overlaps with the HP1 box

2015 ◽  
Vol 462 (3) ◽  
pp. 201-207 ◽  
Author(s):  
Tetsuji Moriyama ◽  
Percival Sangel ◽  
Hiroki Yamaguchi ◽  
Chikashi Obuse ◽  
Yoichi Miyamoto ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Localization Signal ◽  
Identification And Characterization

scholarly journals Characterization of the Putative Transposase mRNA of Tag1, Which Is Ubiquitously Expressed in Arabidopsis and Can Be Induced by Agrobacterium-Mediated Transformation With dTag1 DNA

Genetics ◽  
1998 ◽  
Vol 149 (2) ◽  
pp. 693-701 ◽  
Author(s):  
Dong Liu ◽  
Nigel M Crawford
Keyword(s):  
Arabidopsis Thaliana ◽  
Transposable Element ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Transcript Levels ◽  
Agrobacterium Mediated Transformation ◽  
Transgenic Lines ◽  
Localization Signal ◽  
Transposase Mrna

Abstract Tag1 is an autonomous transposable element of Arabidopsis thaliana. Tag1 expression was examined in two ecotypes of Arabidopsis (Columbia and No-0) that were transformed with CaMV 35S-Tag1-GUS DNA. These ecotypes contain no endogenous Tag1 elements. A major 2.3-kb and several minor transcripts were detected in all major organs of the plants. The major transcript encoded a putative transposase of 84.2 kD with two nuclear localization signal sequences and a region conserved among transposases of the Ac or hAT family of elements. The abundance of Tag1 transcripts varied among transgenic lines and did not correlate with somatic excision frequency or germinal reversion rates, suggesting that factors other than transcript levels control Tag1 excision activity. In untransformed plants of the Landsberg ecotype, which contain two endogenous Tag1 elements, no Tag1 transcripts were detected. Agrobacterium-mediated transformation of these Landsberg plants with a defective 1.4-kb Tag1 element resulted in the appearance of full-length Tag1 transcripts from the endogenous elements. Transformation with control DNA containing no Tag1 sequences did not activate endogenous Tag1 expression. These results indicate that Agrobacterium-mediated transformation with dTag1 can activate the expression of Tag1.

scholarly journals Characterization of a Nuclear Localization Signal of Canine Parvovirus Capsid Proteins

1997 ◽  
Vol 250 (2) ◽  
pp. 389-394 ◽  
Author(s):  
Maija Vihinen-Ranta ◽  
Laura Kakkola ◽  
Anne Kalela ◽  
Pekka Vilja ◽  
Matti Vuento
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Canine Parvovirus ◽  
Capsid Proteins ◽  
Localization Signal

scholarly journals Characterization of the nuclear localization signal of high risk HPV16 E2 protein

Virology ◽  
2007 ◽  
Vol 360 (1) ◽  
pp. 191-198 ◽  
Author(s):  
Kristin Klucevsek ◽  
Mary Wertz ◽  
John Lucchi ◽  
Anna Leszczynski ◽  
Junona Moroianu
Keyword(s):  
High Risk ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
E2 Protein ◽  
Localization Signal

scholarly journals SUMOylation of the Polyglutamine Repeat Protein, Ataxin-1, Is Dependent on a Functional Nuclear Localization Signal

2005 ◽  
Vol 280 (23) ◽  
pp. 21942-21948 ◽  
Author(s):  
Brigit E. Riley ◽  
Huda Y. Zoghbi ◽  
Harry T. Orr
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
High Mobility ◽  
Wild Type ◽  
Repeat Protein ◽  
Polyglutamine Repeat ◽  
Lysine Residues ◽  
Localization Signal ◽  
Functional Nuclear Localization Signal ◽  
Polyglutamine Tract

SUMO (small ubiquitin-like modifier) is a member of the ubiquitin family of proteins. SUMO targets include proteins involved in numerous roles including nuclear transport and transcriptional regulation. The previous finding that mutant ataxin-1[82Q] disrupted promyelocytic leukemia (PML) oncogenic domains prompted us to determine whether ataxin-1 disrupts another component of PML oncogenic domains, Sp100 (100-kDa Speckled protein). Similar to the PML protein, mutant ataxin-1[82Q] redistributed Sp100 to mutant ataxin-1[82Q] nuclear inclusions. Based on the ability of PML and Sp100 to be covalently modified by SUMO, we investigated the ability of ataxin-1 to be SUMOylated. SUMO-1 was found to covalently modify the polyglutamine repeat protein ataxin-1. There was a decrease in ataxin-1 SUMOylation in the presence of the expanded polyglutamine tract, ataxin-1[82Q]. The phospho-mutant, ataxin-1[82Q]-S776A, restored SUMO levels to those of wild-type ataxin-1[30Q]. SUMOylation of ataxin-1 was dependent on a functional nuclear localization signal. Ataxin-1 SUMOylation was mapped to at least five lysine residues. Lys16, Lys194 preceding the polyglutamine tract, Lys610/Lys697 in the C-terminal ataxin high mobility group domain, and Lys746 all contribute to ataxin-1 SUMOylation.

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