scholarly journals A Nuclear Localization Signal Is Essential for Stress-induced Dimer-to-Trimer Transition of Heat Shock Transcription Factor 3

2000 ◽  
Vol 275 (44) ◽  
pp. 34665-34671 ◽  
Author(s):  
Akira Nakai ◽  
Terumi Ishikawa
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Heat Shock Transcription Factor ◽  
Localization Signal ◽  
Transcription Factor 3

Identification of a nuclear localization signal, RRMKWKK, in the homeodomain transcription factor PDX-1

FEBS Letters ◽  
1999 ◽  
Vol 461 (3) ◽  
pp. 229-234 ◽  
Author(s):  
Tilo Moede ◽  
Barbara Leibiger ◽  
Hamedeh Ghanaat Pour ◽  
Per-Olof Berggren ◽  
Ingo B Leibiger
Keyword(s):  
Transcription Factor ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Homeodomain Transcription Factor ◽  
Localization Signal

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 Functional Identification of a Nuclear Localization Signal of MYB2 Protein in Giardia lamblia

2020 ◽  
Vol 58 (6) ◽  
pp. 675-679
Author(s):  
Juri Kim ◽  
Mee Young Shin ◽  
Soon-Jung Park
Keyword(s):  
Transcription Factor ◽  
Amino Acid ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Nuclear Localization Signal ◽  
Giardia Lamblia ◽  
Nuclear Protein ◽  
Functional Identification ◽  
Localization Signal ◽  
Nuclear Location

MYB2 protein was identified as a transcription factor that showed encystation-induced expression in <i>Giardia lamblia</i>. Although nuclear import is essential for the functioning of a transcription factor, an evident nuclear localization signal (NLS) of <i>G. lamblia</i> MYB2 (GlMYB2) has not been defined. Based on putative GlMYB2 NLSs predicted by 2 programs, a series of plasmids expressing hemagglutinin (HA)-tagged GlMYB2 from the promoter of <i>G. lamblia</i> glutamate dehydrogenase were constructed and transfected into Giardia trophozoites. Immunofluorescence assays using anti-HA antibodies indicated that GlMYB2 amino acid sequence #507–#530 was required for the nuclear localization of GlMYB2, and this sequence was named as NLS<sub>GlMYB2</sub>. We further verified this finding by demonstrating the nuclear location of a protein obtained by the fusion of NLS<sub>GlMYB2</sub> and <i>G. lamblia</i> glyceraldehyde 3-phosphate dehydrogenase, a non-nuclear protein. Our data on GlMYB2 will expand our understanding on NLSs functioning in <i>G. lamblia.</i>

scholarly journals Effect of the C.–1 388 A>G polymorphism in chicken heat shock transcription factor 3 gene on heat tolerance

2015 ◽  
Vol 14 (9) ◽  
pp. 1808-1815 ◽  
Author(s):  
Wen-wu ZHANG ◽  
Li-na KONG ◽  
De-xiang ZHANG ◽  
Cong-liang JI ◽  
Xi-quan ZHANG ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Tolerance ◽  
Heat Shock Transcription Factor ◽  
Transcription Factor 3

scholarly journals p53 Suppresses the c-Myb-induced Activation of Heat Shock Transcription Factor 3

2000 ◽  
Vol 275 (20) ◽  
pp. 15578-15585 ◽  
Author(s):  
Jun Tanikawa ◽  
Emi Ichikawa-Iwata ◽  
Chie Kanei-Ishii ◽  
Akira Nakai ◽  
Shu-ichi Matsuzawa ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Transcription Factor 3

scholarly journals Novel missense mutations in the TRPS1 transcription factor define the nuclear localization signal

2003 ◽  
Vol 12 (2) ◽  
pp. 121-126 ◽  
Author(s):  
Frank J Kaiser ◽  
Paola Brega ◽  
Michael L Raff ◽  
Peter H Byers ◽  
Sabina Gallati ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Missense Mutations ◽  
Localization Signal

Nuclear accumulation of the E2F heterodimer regulated by subunit composition and alternative splicing of a nuclear localization signal

1996 ◽  
Vol 109 (10) ◽  
pp. 2443-2452 ◽  
Author(s):  
S. de la Luna ◽  
M.J. Burden ◽  
C.W. Lee ◽  
N.B. La Thangue
Keyword(s):  
Cell Cycle ◽  
Transcription Factor ◽  
Alternative Splicing ◽  
Dna Binding ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Binding Activity ◽  
Nuclear Accumulation ◽  
Dna Binding Activity ◽  
Localization Signal

The cellular transcription factor E2F plays a critical role in integrating cell cycle progression with the transcription apparatus by virtue of a physical interaction and control by key regulators of the cell cycle, such as pRb, cyclins and cyclin-dependent kinases. Generic E2F DNA binding activity arises when a member of two families of proteins, E2F and DP, form heterodimeric complexes, an interaction which results in co-operative transcriptional and DNA binding activity. Here, we characterise a new and hitherto unexpected mechanism of control influencing the activity of E2F which is mediated at the level of intracellular location through a dependence on heterodimer formation for nuclear translocation. Nuclear accumulation is dramatically influenced by two distinct processes: alternative splicing of a nuclear localization signal and subunit composition of the E2F heterodimer. These data define a new level of control in the E2F transcription factor whereby interplay between subunits dictates the levels of nuclear DNA binding activity.

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