Functional characterization of rice CW-domain containing zinc finger proteins involved in histone recognition

Background. We have previously performed an analysis of the cold-responsive transcriptome in the mature leaves of tiger lily (Lilium lancifolium) by gene co-expression network identification. The results has revealed that a ZFHD gene, notated as encoding zinc finger homeodomain protein, may play an essential regulating role in tiger lily response to cold stress. Methods. A further investigation of the ZFHD gene (termed as LlZFHD4) responding to osmotic stresses, including cold, salt, water stresses, and abscisic acid (ABA) was performed in this study. Based on the transcriptome sequences, the coding region and 5′ promoter region of LlZFHD4 were cloned from mature tiger lily leaves. Stress response analysis was performed under continuous 4 °C, NaCl, PEG, and ABA treatments. Functional characterization of LlZFHD4 was conducted in transgenic Arabidopsis, tobacco, and yeast. Results. LlZFHD4 encodes a nuclear-localized protein consisting of 180 amino acids. The N-terminal region of LlZFHD4 has transcriptional activation activity in yeast. The 4 °C, NaCl, PEG, and ABA treatments induced the expression of LlZFHD4. Several stress- or hormone-responsive cis-acting regulatory elements (T-Box, BoxI. and ARF) and binding sites of transcription factors (MYC, DRE and W-box) were found in the core promoter region (789 bp) of LlZFHD4. Also, the GUS gene driven by LlZFHD4 promoter was up-regulated by cold, NaCl, water stresses, and ABA in Arabidopsis. Overexpression of LlZFHD4 improved cold and drought tolerance in transgenic Arabidopsis; higher survival rate and better osmotic adjustment capacity were observed in LlZFHD4 transgenic plants compared to wild type (WT) plants under 4 °C and PEG conditions. However, LlZFHD4 transgenic plants were less tolerant to salinity and more hypersensitive to ABA compared to WT plants. The transcript levels of stress- and ABA-responsive genes were much more up-regulated in LlZFHD4 transgenic Arabidopsis than WT. These results indicate LlZFHD4 is involved in ABA signaling pathway and plays a crucial role in regulating the response of tiger lily to cold, salt and water stresses.

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Cloning and Functional Characterization of Roaz, a Zinc Finger Protein that Interacts with O/E-1 to Regulate Gene Expression: Implications for Olfactory Neuronal Development

Journal of Neuroscience ◽

10.1523/jneurosci.17-11-04159.1997 ◽

1997 ◽

Vol 17 (11) ◽

pp. 4159-4169 ◽

Cited By ~ 96

Author(s):

Robert Y. L. Tsai ◽

Randall R. Reed

Keyword(s):

Gene Expression ◽

Zinc Finger ◽

Neuronal Development ◽

Zinc Finger Protein ◽

Functional Characterization ◽

Regulate Gene Expression ◽

Finger Protein ◽

Regulate Gene

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Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN

Science ◽

10.1126/science.aat0572 ◽

2018 ◽

Vol 362 (6414) ◽

pp. eaat0572 ◽

Cited By ~ 87

Author(s):

Quinlan L. Sievers ◽

Georg Petzold ◽

Richard D. Bunker ◽

Aline Renneville ◽

Mikołaj Słabicki ◽

...

Keyword(s):

Transcription Factors ◽

Small Molecules ◽

Zinc Finger ◽

Ubiquitin Ligase ◽

Biochemical Analysis ◽

Zinc Fingers ◽

Functional Characterization ◽

C2h2 Zinc Finger

The small molecules thalidomide, lenalidomide, and pomalidomide induce the ubiquitination and proteasomal degradation of the transcription factors Ikaros (IKZF1) and Aiolos (IKZF3) by recruiting a Cys2-His2 (C2H2) zinc finger domain to Cereblon (CRBN), the substrate receptor of the CRL4CRBN E3 ubiquitin ligase. We screened the human C2H2 zinc finger proteome for degradation in the presence of thalidomide analogs, identifying 11 zinc finger degrons. Structural and functional characterization of the C2H2 zinc finger degrons demonstrates how diverse zinc finger domains bind the permissive drug-CRBN interface. Computational zinc finger docking and biochemical analysis predict that more than 150 zinc fingers bind the drug-CRBN complex in vitro, and we show that selective zinc finger degradation can be achieved through compound modifications. Our results provide a rationale for therapeutically targeting transcription factors that were previously considered undruggable.

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Characterization of the ZFX family of transcription factors that bind downstream of the start site of CpG island promoters

Nucleic Acids Research ◽

10.1093/nar/gkaa384 ◽

2020 ◽

Vol 48 (11) ◽

pp. 5986-6000 ◽

Cited By ~ 1

Author(s):

Weiya Ni ◽

Andrew A Perez ◽

Shannon Schreiner ◽

Charles M Nicolet ◽

Peggy J Farnham

Keyword(s):

Dna Binding ◽

Zinc Finger ◽

Cpg Island ◽

Zinc Finger Proteins ◽

Double Knockout ◽

Altered Expression ◽

C2h2 Zinc Finger ◽

Necessary And Sufficient ◽

Functional Analyses

Abstract Our study focuses on a family of ubiquitously expressed human C2H2 zinc finger proteins comprised of ZFX, ZFY and ZNF711. Although their protein structure suggests that ZFX, ZFY and ZNF711 are transcriptional regulators, the mechanisms by which they influence transcription have not yet been elucidated. We used CRISPR-mediated deletion to create bi-allelic knockouts of ZFX and/or ZNF711 in female HEK293T cells (which naturally lack ZFY). We found that loss of either ZFX or ZNF711 reduced cell growth and that the double knockout cells have major defects in proliferation. RNA-seq analysis revealed that thousands of genes showed altered expression in the double knockout clones, suggesting that these TFs are critical regulators of the transcriptome. To gain insight into how these TFs regulate transcription, we created mutant ZFX proteins and analyzed them for DNA binding and transactivation capability. We found that zinc fingers 11–13 are necessary and sufficient for DNA binding and, in combination with the N terminal region, constitute a functional transactivator. Our functional analyses of the ZFX family provides important new insights into transcriptional regulation in human cells by members of the large, but under-studied family of C2H2 zinc finger proteins.

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Solution structures and characterization of human immunodeficiency virus Rev responsive element IIB RNA targeting zinc finger proteins

Biopolymers ◽

10.1002/bip.20565 ◽

2006 ◽

Vol 83 (4) ◽

pp. 352-364 ◽

Cited By ~ 4

Author(s):

Subrata H. Mishra ◽

Christopher M. Shelley ◽

Doyle J. Barrow ◽

Martyn K. Darby ◽

Markus W. Germann

Keyword(s):

Human Immunodeficiency Virus ◽

Zinc Finger ◽

Zinc Finger Proteins ◽

Solution Structures ◽

Rna Targeting ◽

Immunodeficiency Virus ◽

Responsive Element

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A gene that encodes a protein consisting solely of zinc finger domains is preferentially expressed in transformed mouse cells

Molecular and Cellular Biology ◽

10.1128/mcb.10.1.418-421.1990 ◽

1990 ◽

Vol 10 (1) ◽

pp. 418-421

Author(s):

M Ernoult-Lange ◽

M Kress ◽

D Hamer

Keyword(s):

Amino Acids ◽

Brain Tissue ◽

Zinc Finger ◽

Cellular Transformation ◽

Zinc Finger Proteins ◽

Mouse Cells ◽

Zinc Finger Domains ◽

Transformed Cell Lines ◽

Testis Tissue

We describe the cloning and characterization of the mouse MOK-2 gene, a new member of the Krüppel family of zinc finger proteins. Sequencing of both cDNA and genomic clones showed that the predicted MOK-2 protein consists of seven zinc finger domains with only five additional amino acids. The finger domains of MOK-2 are highly homologous to one another but not to those of other zinc finger proteins. MOK-2 is preferentially expressed in transformed cell lines, brain tissue, and testis tissue. Its possible role in cellular transformation is discussed.

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