scholarly journals Nuclear localization, DNA binding and restricted expression in neural and germ cells of zebrafish Dmrt3

2008 ◽  
Vol 100 (8) ◽  
pp. 453-463 ◽  
Author(s):  
Qin Li ◽  
Xiang Zhou ◽  
Yiqing Guo ◽  
Xuan Shang ◽  
Hao Chen ◽  
...  
Keyword(s):  
Dna Binding ◽  
Nuclear Localization ◽  
Germ Cells

scholarly journals Human GATA-3 trans-activation, DNA-binding, and nuclear localization activities are organized into distinct structural domains.

1994 ◽  
Vol 14 (3) ◽  
pp. 2201-2212 ◽  
Author(s):  
Z Yang ◽  
L Gu ◽  
P H Romeo ◽  
D Bories ◽  
H Motohashi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Structural Domains ◽  
Cellular Genes ◽  
Dna Binding Site ◽  
Discrete Domains ◽  
Definition Of ◽  
Site Recognition

GATA-3 is a zinc finger transcription factor which is expressed in a highly restricted and strongly conserved tissue distribution pattern in vertebrate organisms, specifically, in a subset of hematopoietic cells, in cells within the central and peripheral nervous systems, in the kidney, and in placental trophoblasts. Tissue-specific cellular genes regulated by GATA-3 have been identified in T lymphocytes and the placenta, while GATA-3-regulated genes in the nervous system and kidney have not yet been defined. We prepared monoclonal antibodies with which we could dissect the biochemical and functional properties of human GATA-3. The results of these experiments show some anticipated phenotypes, for example, the definition of discrete domains required for specific DNA-binding site recognition (amino acids 303 to 348) and trans activation (amino acids 30 to 74). The signaling sequence for nuclear localization of human GATA-3 is a property conferred by sequences within and surrounding the amino finger (amino acids 249 to 311) of the protein, thereby assigning a function to this domain and thus explaining the curious observation that this zinc finger is dispensable for DNA binding by the GATA family of transcription factors.

scholarly journals A novel nuclear localization signal spans the linker of the two DNA-binding subdomains in the conserved paired domain of Pax6

2018 ◽  
Vol 93 (2) ◽  
pp. 75-81 ◽  
Author(s):  
Hiromasa Tabata ◽  
Akihiro Koinui ◽  
Atsushi Ogura ◽  
Daisuke Nishihara ◽  
Hiroaki Yamamoto
Keyword(s):  
Dna Binding ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Paired Domain ◽  
Localization Signal

Human GATA-3 trans-activation, DNA-binding, and nuclear localization activities are organized into distinct structural domains

1994 ◽  
Vol 14 (3) ◽  
pp. 2201-2212
Author(s):  
Z Yang ◽  
L Gu ◽  
P H Romeo ◽  
D Bories ◽  
H Motohashi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Structural Domains ◽  
Cellular Genes ◽  
Dna Binding Site ◽  
Discrete Domains ◽  
Definition Of ◽  
Site Recognition

GATA-3 is a zinc finger transcription factor which is expressed in a highly restricted and strongly conserved tissue distribution pattern in vertebrate organisms, specifically, in a subset of hematopoietic cells, in cells within the central and peripheral nervous systems, in the kidney, and in placental trophoblasts. Tissue-specific cellular genes regulated by GATA-3 have been identified in T lymphocytes and the placenta, while GATA-3-regulated genes in the nervous system and kidney have not yet been defined. We prepared monoclonal antibodies with which we could dissect the biochemical and functional properties of human GATA-3. The results of these experiments show some anticipated phenotypes, for example, the definition of discrete domains required for specific DNA-binding site recognition (amino acids 303 to 348) and trans activation (amino acids 30 to 74). The signaling sequence for nuclear localization of human GATA-3 is a property conferred by sequences within and surrounding the amino finger (amino acids 249 to 311) of the protein, thereby assigning a function to this domain and thus explaining the curious observation that this zinc finger is dispensable for DNA binding by the GATA family of transcription factors.

scholarly journals Nuclear localization of a DNA-binding C-terminal domain from Balbiani ring coded secretory protein.

1988 ◽  
Vol 7 (12) ◽  
pp. 3881-3888 ◽  
Author(s):  
L. Botella ◽  
C. Grond ◽  
H. Saiga ◽  
J. E. Edström
Keyword(s):  
Dna Binding ◽  
Nuclear Localization ◽  
Secretory Protein ◽  
Balbiani Ring ◽  
Terminal Domain

scholarly journals A specific and unusual nuclear localization signal in the DNA binding domain of the Rev-erb orphan receptors

2003 ◽  
Vol 30 (2) ◽  
pp. 197-211 ◽  
Author(s):  
S Chopin-Delannoy ◽  
S Thenot ◽  
F Delaunay ◽  
E Buisine ◽  
A Begue ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Fusion Protein ◽  
Nuclear Receptors ◽  
Nuclear Localization ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Protein Fusion ◽  
Orphan Receptors ◽  
Amino Terminal

The orphan receptors Rev-erbalpha and Rev-erbbeta are members of the nuclear receptors superfamily and act as transcriptional repressors. Rev-erbalpha is expressed with a robust circadian rhythm and is involved in liver metabolism through repression of the ApoA1 gene, but no role has been yet defined for Rev-erbbeta. To gain better understanding of their function and mode of action, we characterized the proteins encoded by these two genes. Both Rev-erbalpha and Rev-erbbeta proteins were nuclear when transiently transfected in COS-1 cells. The major nuclear location signal (NLS) of Rev-erbalpha is in the amino-terminal region of the protein. Fusion of green fluorescent protein (GFP) to the amino terminus of Rev-erbalpha deletion mutants showed that the NLS is located within a 53 amino acid segment of the DNA binding domain (DBD). The homologous region of Rev-erbbeta fused to GFP also targeted the fusion protein to the nucleus, suggesting that the location of this NLS is conserved among all the Rev-erb group members. Interestingly, members of the phylogenetically closest nuclear orphan receptor group (ROR), which exhibit 58% amino acid identity with Rev-erb in the DBD, do not have their NLS located within the DBD. GFP/DBD. RORalpha or GFP/DBD.RORbeta remained cytoplasmic, in contrast to GFP/DBD. Rev-erb fusion proteins. Alignment of human Rev-erb and ROR DBD amino acid sequences predicted that the two basic residues, K167 and R168, located just upstream from the second zinc finger, could play a critical part in the nuclear localization of Rev-erb proteins. Substitution of these two residues with those found in ROR, in the GFP/DBD. Rev-erb context, resulted in cytoplasmic proteins. In contrast, the reverse mutation of the GFP/DBD. RORalpha towards the Rev-erbalpha residues targeted the fusion protein to the nucleus. Our data demonstrate that Rev-erb proteins contain a functional NLS in the DBD. Its location is unusual within the nuclear receptor superfamily and suggests that Rev-erb orphan receptors control their intracellular localization via a mechanism different from that of other nuclear receptors.

scholarly journals A Highly Organized Structure Mediating Nuclear Localization of a Myb2 Transcription Factor in the Protozoan Parasite Trichomonas vaginalis

2011 ◽  
Vol 10 (12) ◽  
pp. 1607-1617 ◽  
Author(s):  
Chien-Hsin Chu ◽  
Lung-Chun Chang ◽  
Hong-Ming Hsu ◽  
Shu-Yi Wei ◽  
Hsing-Wei Liu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Trichomonas Vaginalis ◽  
Simian Virus 40 ◽  
Binding Activity ◽  
T Antigen ◽  
Structural Domain ◽  
Dna Binding Activity

ABSTRACT Nuclear proteins usually contain specific peptide sequences, referred to as nuclear localization signals (NLSs), for nuclear import. These signals remain unexplored in the protozoan pathogen, Trichomonas vaginalis . The nuclear import of a Myb2 transcription factor was studied here using immunodetection of a hemagglutinin-tagged Myb2 overexpressed in the parasite. The tagged Myb2 was localized to the nucleus as punctate signals. With mutations of its polybasic sequences, 48KKQK51 and 61KR62, Myb2 was localized to the nucleus, but the signal was diffusive. When fused to a C-terminal non-nuclear protein, the Myb2 sequence spanning amino acid (aa) residues 48 to 143, which is embedded within the R2R3 DNA-binding domain (aa 40 to 156), was essential and sufficient for efficient nuclear import of a bacterial tetracycline repressor (TetR), and yet the transport efficiency was reduced with an additional fusion of a firefly luciferase to TetR, while classical NLSs from the simian virus 40 T-antigen had no function in this assay system. Myb2 nuclear import and DNA-binding activity were substantially perturbed with mutation of a conserved isoleucine (I74) in helix 2 to proline that altered secondary structure and ternary folding of the R2R3 domain. Disruption of DNA-binding activity alone by point mutation of a lysine residue, K51, preceding the structural domain had little effect on Myb2 nuclear localization, suggesting that nuclear translocation of Myb2, which requires an ordered structural domain, is independent of its DNA binding activity. These findings provide useful information for testing whether myriad Mybs in the parasite use a common module to regulate nuclear import.

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