scholarly journals A constitutive nuclear localization signal from the second zinc-finger of orphan nuclear receptor TR2

1998 ◽  
Vol 159 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Z Yu ◽  
CH Lee ◽  
C Chinpaisal ◽  
LN Wei
Keyword(s):  
Nuclear Receptor ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Fluorescent Protein ◽  
Biologically Active ◽  
Binding Property ◽  
Orphan Nuclear Receptor ◽  
Mobility Shift ◽  
Localization Signal

The orphan nuclear receptor TR2 and its truncated isoform deleted in the ligand binding domain (LBD) were localized exclusively in the nuclei as revealed by two methods of detection. An anti-hemagglutinin (HA) antibody detected specific nuclear localization of HA-tagged receptors and the green fluorescent protein (GFP)-tagged receptors were found to be distributed in the nuclei of living cells. By deletion analyses, the sequence responsible for targeting this receptor into the nucleus was defined. A stretch of 20 amino acid residues (KDCVINKHHRNRCQYCRLQR) within the second zinc-finger of this receptor is required for its nuclear localization and this signal is constitutively active. No nuclear localization signal was found in the N-terminus or the LBD. The GFP-tagged receptor remained biologically active, as evidenced by its repressive activity on the reporter that carried a binding site for this receptor, a direct repeat-5 (DR5). An electrophoretic mobility shift assay was performed to characterize the binding property of TR2 and its truncated isoform. TR2 bound to the DR5 as dimers whereas its truncated isoform bound as monomers.

Xenopus nuclear factor 7 (xnf7) possesses an NLS that functions efficiently in both oocytes and embryos

1993 ◽  
Vol 105 (2) ◽  
pp. 389-395
Author(s):  
X. Li ◽  
L.D. Etkin
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Nuclear Accumulation ◽  
Nuclear Factor ◽  
Zinc Finger Gene ◽  
Early Embryos ◽  
Localization Signal ◽  
Nuclear Phosphoprotein

Xenopus nuclear factor 7 (xnf7) is a nuclear phosphoprotein that is encoded by a member of a novel zinc finger gene family and likely functions as a transcription factor. It possesses a nuclear localization signal (NLS) similar to the bipartite basic NLS of nucleoplasmin, but unlike nucleoplasmin, which re-enters nuclei immediately after fertilization, xnf7 remains cytoplasmic until the mid-blastula transition (MBT). We have measured the accumulation of injected labeled xnf7 protein or protein produced from synthetic xnf7 transcripts in the oocyte nuclei (GV). The data show that the NLS of xnf7 functions efficiently in oocytes. Mutations in either of the bipartite basic domains of the xnf7 NLS inhibit nuclear accumulation, while mutations in the spacer sequences have no effect. The xnf7 NLS linked to pyruvate kinase directs the efficient accumulation of this protein into nuclei of early embryos prior to the MBT. These data suggest that retention of the xnf7 protein during development is the result of a mechanism that interferes with the xnf7 NLS function.

scholarly journals Identification of nuclear localization signals in the human homeoprotein MSX1

2018 ◽  
Vol 96 (4) ◽  
pp. 483-489 ◽  
Author(s):  
Akio Shibata ◽  
Junichiro Machida ◽  
Seishi Yamaguchi ◽  
Masashi Kimura ◽  
Tadashi Tatematsu ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Fluorescent Protein ◽  
Nuclear Accumulation ◽  
Web Based ◽  
Core Motif ◽  
Nuclear Localization Signals ◽  
Proliferation And Differentiation ◽  
Localization Signal ◽  
Green Fluorescent

MSX1 is one of the homeoproteins with the homeodomain (HD) sequence, which regulates proliferation and differentiation of mesenchymal cells. In this study, we investigated the nuclear localization signal (NLS) in the MSX1 HD by deletion and amino acid substitution analyses. The web-based tool NLStradamus predicted 2 putative basic motifs in the N- and C-termini of the MSX1 HD. Green fluorescent protein (GFP) chimera studies revealed that NLS1 (161RKHKTNRKPR170) and NLS2 (216NRRAKAKR223) were independently insufficient for robust nuclear localization. However, they can work cooperatively to promote nuclear localization of MSX1, as was shown by the 2 tandem NLS motifs partially restoring functional NLS, leading to a significant nuclear accumulation of the GFP chimera. These results demonstrate a unique NLS motif in MSX1, which consists of an essential single core motif in helix-I, with weak potency, and an auxiliary subdomain in helix-III, which alone does not have nuclear localization potency. Additionally, other peptide sequences, other than predicted 2 motifs in the spacer, may be necessary for complete nuclear localization in MSX1 HD.

scholarly journals Functional Characterization of the Nuclear Localization Signal for a Suppressor of Posttranscriptional Gene Silencing

2003 ◽  
Vol 77 (12) ◽  
pp. 7026-7033 ◽  
Author(s):  
Xiangli Dong ◽  
Rene van Wezel ◽  
John Stanley ◽  
Yiguo Hong
Keyword(s):  
Amino Acid ◽  
Gene Silencing ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Fluorescent Protein ◽  
Functional Characterization ◽  
Potato Virus X ◽  
Posttranscriptional Gene Silencing ◽  
Arginine Residues ◽  
Localization Signal

ABSTRACT The nucleus-localized C2 protein of Tomato yellow leaf curl virus-China (TYLCV-C) is an active suppressor of posttranscriptional gene silencing (PTGS). Consistently, infection with TYLCV-C resulted in PTGS arrest in plants. The C2 protein possesses a functional, arginine-rich nuclear localization signal within the basic amino acid-rich region 17KVQHRIAKKTTRRRR31. When expressed from potato virus X, C2-RRRR31DVGG (in which the four consecutive arginine residues 28RRRR31 were replaced with DVGG) that had been tagged with a green fluorescent protein (GFP) failed to transport GFP into nuclei and was dysfunctional in inducing necrosis and suppressing PTGS in plants. Amino acid substitution mutants C2-K17D-GFP, C2-HR21DV-GFP, and C2-KK25DI-GFP localized to nuclei and produced necrosis, but only C2-K17D-GFP suppressed PTGS. The N-terminal portions C21-31 and C217-31 fused in frame to GFP were capable of targeting GFP to nuclei, but neither caused necrosis nor affected PTGS. Our data establish that nuclear localization is likely required for C2 protein to function in C2-mediated induction of necrosis and suppression of PTGS, which may follow diverse pathways in plants. Possible mechanisms of how the C2 protein involves these biological functions are discussed.

scholarly journals Functional and structural basis of the nuclear localization signal in the ZIC3 zinc finger domain

2008 ◽  
Vol 17 (22) ◽  
pp. 3459-3473 ◽  
Author(s):  
Minoru Hatayama ◽  
Tadashi Tomizawa ◽  
Kumiko Sakai-Kato ◽  
Patrice Bouvagnet ◽  
Shingo Kose ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Structural Basis ◽  
Zinc Finger Domain ◽  
Localization Signal

scholarly journals Zinc finger domain of Snail functions as a nuclear localization signal for importin β-mediated nuclear import pathway

2005 ◽  
Vol 10 (5) ◽  
pp. 455-464 ◽  
Author(s):  
Hideki Yamasaki ◽  
Toshihiro Sekimoto ◽  
Tadashi Ohkubo ◽  
Tsutomu Douchi ◽  
Yukihiro Nagata ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Nuclear Localization Signal ◽  
Zinc Finger Domain ◽  
Localization Signal
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