TY - JOUR. T1 - Custom DNA-binding proteins come of age. T2 - Polydactyl zinc-finger proteins. AU - Segal, David. AU - Barbas, Carlos F.. PY - 2001/12/1. Y1 - 2001/12/1. N2 - Artificial transcription factors based on modified zinc-finger DNA-binding domains have been shown to activate or repress the transcription of endogenous genes in multiple organisms. Advances in both the construction of novel zinc-finger proteins and our understanding of the characteristics of a productive regulatory site have fueled these achievements.. AB - Artificial transcription factors based on modified zinc-finger DNA-binding domains have been shown to activate or repress the transcription of endogenous genes in multiple organisms. Advances in both the construction of novel zinc-finger proteins and our understanding of the characteristics of a productive regulatory site have fueled these achievements.. UR - http://www.scopus.com/inward/record.url?scp=0035712253&partnerID=8YFLogxK. UR - ...
Zinc-finger nucleases (ZFNs) are artificial restriction enzymes generated by fusing a zinc finger DNA-binding domain to a DNA-cleavage domain. Zinc finger domains can be engineered to target specific desired DNA sequences and this enables zinc-finger nucleases to target unique sequences within complex genomes. By taking advantage of endogenous DNA repair machinery, these reagents can be used to precisely alter the genomes of higher organisms. Alongside CRISPR/Cas9 and TALEN, ZFN is a prominent tool in the field of genome editing. The DNA-binding domains of individual ZFNs typically contain between three and six individual zinc finger repeats and can each recognize between 9 and 18 basepairs. If the zinc finger domains perfectly recognize a 3 basepair DNA sequence to generate a 3-finger array that can recognize a 9 basepair target site. Other procedures can utilize either 1-finger or 2-finger modules to generate zinc-finger arrays with six or more individual zinc fingers. The main drawback with ...
Read "Functions of the CCCH type zinc finger protein OsGZF1 in regulation of the seed storage protein GluB-1 from rice, Plant Molecular Biology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
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A zinc finger motif is an element of proteins that can specifically recognize and bind to DNA. Because they contain multiple cysteine residues, zinc finger motifs possess redox properties. Ionizing radiation generates a variety of free radicals in organisms. Zinc finger motifs, therefore, may be a target of ionizing radiation. The effect of gamma radiation on the zinc finger motifs in transcription factor IIIA (TFIIIA), a zinc finger protein, was investigated. TFIIIA was exposed to different gamma doses from 60Co sources. The dose rates were 0.20 Gy/min and 800 Gy/h, respectively. The binding capacity of zinc finger motifs in TFIIIA was determined using an electrophoretic mobility shift assay. We found that 1000 Gy of gamma radiation impaired the function of the zinc finger... motifs in TFIIIA. The sites of radiation-induced damage in the zinc finger were the thiol groups of cysteine residues and zinc (II) ions. The thiol groups were oxidized to form disulfide bonds and the zinc (II) ions were ...
TY - JOUR. T1 - Differentiation dependent expression in muscle cells of ZT3, a novel zinc finger factor differentially expressed in embryonic and adult tissues. AU - Polimeni, M.. AU - Giorgi, S.. AU - De Gregorio, L.. AU - Dragani, T. A.. AU - Molinaro, M.. AU - Cossu, G.. AU - Bouché, M.. PY - 1996/1. Y1 - 1996/1. N2 - ZT3, isolated from a murine muscle cell cDNA library by a low-stringency hybridization, encodes a zinc finger domain containing factor with a transcript of 5.0 kb. A 3 2.5 kb partial nucleotide sequence contains an ORF of 1.5 kb where 17 canonical C2H2 zinc finger domains organized in tandem were identified. It maps on mouse chromosome 11, close to two mutations which affect skeletal formation. ZT3 expression depends upon differentiation of myogenic cells in culture, since it is upregulated with myogenin and inhibited in scr-transfected C2C12 cells. ZT3 is not expressed in NIH3T3 or C3H10T1/2 fibroblasts, but is induced when fibroblasts are myogenically converted by ...
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The corpus luteum (CL) is a temporary organ involved in the maintenance of pregnancy. In the course of its life-cycle, the CL undergoes two distinct and consecutive processes for its inevitable removal through apoptosis: functional and structural luteolysis. We isolated a gene encoding for a novel rat zinc finger protein (ZFP), named rat ZFP96 (rZFP96) from an ovarian lambda cDNA library. Sequence analysis revealed close sequence and structural similarity to mouse ZFP96 and human zinc finger protein 305 (ZNF305). Quantitative reverse transcription-polymerase chain reaction analysis revealed a positive correlation with the end of pregnancy, that is, the onset of structural luteolysis of the CL. Messenger RNA levels increased 3-fold (P < 0.01) between days 13 and 22 of pregnancy and 8-fold (P < 0.01) between day 13 of pregnancy and day 1 post-partum. In addition, we detected rZFP96 expression in mammary, placenta, heart, kidney and skeletal muscle. Sequence analysis predicted that rZFP96 has a ...
Zinc finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc finger proteins contain a Krueppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger protein 75 (ZNF75), also known as ZNF82, is a 289 amino acid member of the Krueppel C2H2-type zinc finger protein family. Localized to the nucleus, ZNF75 contains five C2H2- type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation ...
Zinc finger inhibitors, or zinc ejectors, are substances or compounds that interact adversely with zinc fingers and cause them to release their zinc from its binding site, disrupting the conformation of the polypeptide chain and rendering the zinc fingers ineffective, thereby preventing them from performing their associated cellular functions. This is typically accomplished through chelation of the zinc binding site. As zinc fingers are known to be involved in m-RNA regulation, reverse transcription, protection of synthesized viral DNA, transcription inhibition, and initial integration processes, prevention of zinc finger function can have drastic effects on the function of the cell or virus. Zinc finger inhibitors are typically used to combat HIV. HIV treatments usually rely on targeting reverse transcriptases and proteases. However, these methods are proving to be ineffective due to the development of resistant strains of the virus or due to the stoppage of the treatment. This method of using ...
Zinc finger nucleases (ZFNs) are associated with cell death and apoptosis by binding at countless undesired locations. This cytotoxicity is associated with the binding ability of engineered zinc finger domains to bind dissimilar DNA sequences with high affinity. In general, binding preferences of transcription factors are associated with significant degenerated diversity and complexity which convolutes the design and engineering of precise DNA binding domains. Evolutionary success of natural zinc finger proteins, however, evinces that nature created specific evolutionary traits and strategies, such as modularity and rank-specific recognition to cope with binding complexity that are critical for creating clinical viable tools to precisely modify the human genome. Our findings indicate preservation of general modularity and significant alteration of the rank-specific binding preferences of the three-finger binding domain of transcription factor SP1 when exchanging amino acids in the 2nd finger. ...
BACKGROUND ZNF32 has been predicted to be a zinc finger protein and is involved in cell differentiation and tumor development, but its precise function is unknown. Specific monoclonal antibodies (mAbs) have been widely used in research and clinical diagnosis and treatments. Therefore, we established an anti-ZNF32 mAb to characterize this proteins function. MATERIAL/METHODS Peptide⁴⁹⁻⁶³, a specific small peptide of ZNF32, was chosen and the synthetic keyhole limpet hemocyanin (KLH)-peptide⁴⁹⁻⁶³ was used as an antigen to immunize mice. A mAb against peptide⁴⁹⁻⁶³ was generated by hybridoma technology, and hybridoma cells were screened by limiting dilution. The isoform of mAb-pZNF32-8D9 was identified by double agar diffusion. The sensitivity and specificity of the mAb and expressed levels of ZNF32 in various cells and tissues were identified by enzyme-linked immunosorbent assay (ELISA), immunocytochemistry, immunohistochemistry, and Western blotting. RESULTS A stable anti
Plasmids for genome engineering using zinc finger nucleases (ZFN) constructed via modular assembly of artificial zinc finger arrays.
We report here an efficient method for targeted mutagenesis of Arabidopsis genes through regulated expression of zinc finger nucleases (ZFNs)-enzymes engineered to create DNA double-strand breaks at specific target loci. ZFNs recognizing the Arabidopsis ADH1 and TT4 genes were made by Oligomerized Pool ENgineering (OPEN)-a publicly available, selection-based platform that yields high quality zinc finger arrays. The ADH1 and TT4 ZFNs were placed under control of an estrogen-inducible promoter and introduced into Arabidopsis plants by floral-dip transformation. Primary transgenic Arabidopsis seedlings induced to express the ADH1 or TT4 ZFNs exhibited somatic mutation frequencies of 7% or 16%, respectively. The induced mutations were typically insertions or deletions (1-142 bp) that were localized at the ZFN cleavage site and likely derived from imprecise repair of chromosome breaks by nonhomologous end-joining. Mutations were transmitted to the next generation for 69% of primary transgenics expressing the
The maize INDETERMINATE1 gene, ID1, is a key regulator of the transition to flowering and the founding member of a transcription factor gene family that encodes a protein with a distinct arrangement of zinc finger motifs. The zinc fingers and surrounding sequence make up the signature ID domain (IDD), which appears to be found in all higher plant genomes. The presence of zinc finger domains and previous biochemical studies showing that ID1 binds to DNA suggests that members of this gene family are involved in transcriptional regulation. Comparison of IDD genes identified in Arabidopsis and rice genomes, and all IDD genes discovered in maize EST and genomic databases, suggest that ID1 is a unique member of this gene family. High levels of sequence similarity amongst all IDD genes from maize, rice and Arabidopsis suggest that they are derived from a common ancestor. Several unique features of ID1 suggest that it is a divergent member of the maize IDD family. Although no clear ID1 ortholog was identified
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Zinc finger proteins (ZNFs) bind DNA and, through this binding, regulate gene transcription. Most ZNFs contain conserved C2H2 motifs and are classified as Kruppel-type zinc fingers. For a general description of these proteins, see ZNF91 (MIM 603971).[supplied by OMIM, Jul 2002]
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Blimp1, a zinc-finger containing DNA-binding transcriptional repressor, functions as a master regulator of B cell terminal differentiation. Considerable evidence suggests that Blimp1 is required for the establishment of anteroposterior axis formation and the formation of head structures during early vertebrate development. In mouse embryos, Blimp1 is strongly expressed in axial mesendoderm, the tissue known to provide anterior patterning signals during gastrulation. Here, we describe for the first time the defects caused by loss of Blimp1 function in the mouse. Blimp1 deficient embryos die at mid-gestation, but surprisingly early axis formation, anterior patterning and neural crest formation proceed normally. Rather, loss of Blimp1 expression disrupts morphogenesis of the caudal branchial arches and leads to a failure to correctly elaborate the labyrinthine layer of the placenta. Blimp1 mutant embryos also show widespread blood leakage and tissue apoptosis, and, strikingly, Blimp1 homozygous mutants
TY - JOUR. T1 - An internal deletion within an 11p13 zinc finger gene contributes to the development of Wilms tumor. AU - Haber, Daniel A.. AU - Buckler, Alan J.. AU - Glaser, Thomas M. AU - Call, Katherine M.. AU - Pelletier, Jerry. AU - Sohn, Robert L.. AU - Douglass, Edwin C.. AU - Housman, David E.. PY - 1990/6/29. Y1 - 1990/6/29. N2 - We have recently described the isolation of a candidate for the Wilms tumor susceptibility gene mapping to band p13 of human chromosome 11. This gene, primarily expressed in fetal kidney, appears to encode a DNA binding protein. We now describe a sporadic, unilateral Wilms tumor in which one allele of this gene contains a 25 bp deletion spanning an exon-intron junction and leading to aberrant mRNA splicing and loss of one of the four zinc finger consensus domains in the protein. The mutation is absent in the affected individuals germline, consistent with the somatic inactivation of a tumor suppressor gene. In addition to this intragenic deletion affecting ...
We have previously reported (Villa et al. (1993), Genomics 18: 223) the characterization of the human ZNF75 gene located on Xq26, which has only limited homology (less than 65%) to other ZF genes in the databases. Here, we describe three human zinc finger genes with 86 to 95% homology to ZNF75 at the nucleotide level, which represent all the members of the human ZNF75 subfamily. One of these, ZNF75B, is a pseudogene mapped to chromosome 12q13. The other two, ZNF75A and ZNF75C, maintain an ORF in the sequenced region, and at least the latter is expressed in the U937 cell line. They were mapped to chromosomes 16 and 11, respectively. All these genes are conserved in chimpanzees, gorillas, and orangutans. The ZNF75B homologue is a pseudogene in all three great apes, and in chimpanzee it is located on chromosome 10 (phylogenetic XII), at p13 (corresponding to the human 12q13). The chimpanzee homologue of ZNF75 is also located on the Xq26 chromosome, in the same region, as detected by in situ ...
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An inducible program of inflammatory gene expression is a hallmark of antimicrobial defenses. This response is controlled by a collaboration involving signal-dependent activation of transcription factors, transcriptional co-regulators, and chromatin-modifying factors. Here we have identified a highly conserved Zinc finger DNA binding protein CNBP (also called ZNF9) upregulated in myeloid cells exposed to lipopolysaccharide. CNBP resides primarily in the cytosol and upon TLR4 engagement, CNBP translocate to the nucleus. To investigate the functional consequences of these events, we generated mice lacking CNBP and characterized the role of CNBP in controlling the inducible transcriptional program using a combination of RNA-sequencing and multiplex gene expression analysis (Nanostring). In response to an array of signals such as LPS, CNBP-deficient macrophages were impaired in their ability to induce important immune genes including IL12p40 and IL6 amongst others. CNBP-deficient cells showed normal ...
EntrezGene ,Full_name_from_nomenclature_authority=CCCTC-binding factor (zinc finger protein) ,GeneID=10664 ,LocusTag=- ,Modification_date=20120108 ,Nomenclature_status=O ,Other_designations=11 zinc finger transcriptional repressor;;11-zinc finger protein;;CTCFL paralog;;transcriptional repressor CTCF ,Symbol=CTCF ,Symbol_from_nomenclature_authority=CTCF ,Synonyms=- ,chromosome=16 ,dbXrefs=HGNC:13723;;MIM:604167;;Ensembl:ENSG00000102974;;HPRD:05005;;Vega:OTTHUMG00000137539;;EpiFactors:10664:genes ,description=CCCTC-binding factor (zinc finger protein) ,map_location=16q21-q22.3 ,tax_id=9606 ,tf?=yes ,transcription_factor= ,type_of_gene=protein-coding ...
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The H3K9me3 histone modification is often found at promoter regions, where it functions to repress transcription. However, we have previously shown that 3′ exons of zinc finger genes (ZNFs) are marked by high levels of H3K9me3. We have now further investigated this unusual location for H3K9me3 in ZNF genes. Neither bioinformatic nor experimental approaches support the hypothesis that the 3′ exons of ZNFs are promoters. We further characterized the histone modifications at the 3′ ZNF exons and found that these regions also contain H3K36me3, a mark of transcriptional elongation. A genome-wide analysis of ChIP-seq data revealed that ZNFs constitute the majority of genes that have high levels of both H3K9me3 and H3K36me3. These results suggested the possibility that the ZNF genes may be imprinted, with one allele transcribed and one allele repressed. To test the hypothesis that the contradictory modifications are due to imprinting, we used a SNP analysis of RNA-seq data to demonstrate that both
Zinc finger CCHC domain-containing protein 8 contains a PF00098 domain.. Zinc finger CCHC domain-containing protein 8 contains a PF04046 domain.. Zinc finger CCHC domain-containing protein 8 is proteolytically cut by granzyme B, human-type (S01.010) cleavage. MDED-ALTL.. ...
TY - JOUR. T1 - Egr3/Pilot, a zinc finger transcription factor, is rapidly regulated by activity in brain neurons and colocalizes with Egr1/zif268. AU - Yamagata, K.. AU - Kaufmann, W. E.. AU - Lanahan, A.. AU - Papapavlou, M.. AU - Barnes, Carol A. AU - Andreasson, K. I.. AU - Worley, P. F.. PY - 1994/7. Y1 - 1994/7. UR - http://www.scopus.com/inward/record.url?scp=0028466211&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0028466211&partnerID=8YFLogxK. M3 - Article. C2 - 10467592. AN - SCOPUS:0028466211. VL - 1. SP - 140. EP - 152. JO - Learning and Memory. JF - Learning and Memory. SN - 1072-0502. IS - 2. ER - ...
TY - JOUR. T1 - Zinc finger protein 131 inhibits estrogen signaling by suppressing estrogen receptor α homo-dimerization. AU - Oh, Yohan. AU - Chung, Kwang Chul. PY - 2013/1/4. Y1 - 2013/1/4. N2 - Steroid hormone estrogen elicits various physiological functions, many of which are mediated through two structurally and functionally distinct estrogen receptors, ERα and ERβ. The functional role of zinc finger protein 131 (ZNF131) is poorly understood, but it is assumed to possess transcriptional regulation activity due to the presence of a DNA binding motif. A few recent reports, including ours, revealed that ZNF131 acts as a negative regulator of ERα and that SUMO modification potentiates the negative effect of ZNF131 on estrogen signaling. However, its molecular mechanism for ERα inhibition has not been elucidated in detail. Here, we demonstrate that ZNF131 directly interacts with ERα, which consequently inhibits ERα-mediated trans-activation by suppressing its homo-dimerization. Moreover, ...
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Artificial transcription factors can be engineered to interact with specific DNA sequences to modulate endogenous gene expression within cells. A significant hurdle to implementation of this approach is the selection of the appropriate DNA sequence for targeting. We reasoned that a good target site should be located in chromatin, where it is accessible to DNA-binding proteins, and it should be, in the close vicinity of known transcriptional regulators of the gene. Here we have explored the efficacy of these criteria to guide our selection of potential regulators of gamma-globin expression. Several zinc finger-based transcriptional activators were designed to target the sites proximal to the -117-position of the gamma-globin promoter. This region is proximal to the binding sites of known and potential natural transcription factors. Design and study of three transcription factors identified the potent transcriptional activator, ggl-VP64-RA. This transcription factor was able to interact directly ...
Sangamo BioSciences, Inc. is focused on research and development of novel DNA-binding proteins for therapeutic gene regulation and genome editing. The Company has ongoing Phase 2 clinical trials to evaluate the safety and efficacy of a novel ZFP Therapeutic® for the treatment of HIV/AIDS. Sangamos other therapeutic programs are focused on monogenic diseases, including hemophilia, Huntingtons disease and hemoglobinopathies such as sickle cell anemia and beta-thalassemia. Sangamos core competencies enable the engineering of a class of DNA-binding proteins known as zinc finger DNA-binding proteins (ZFPs). Engineering of ZFPs that recognize a specific DNA sequence enables the creation of sequence-specific ZFP Nucleases (ZFNs) for gene modification and ZFP transcription factors (ZFP TFs) that can control gene expression and, consequently, cell function. Sangamo has entered into a strategic collaboration with Shire AG to develop therapeutics for hemophilia, Huntingtons disease and other monogenic ...
Direct editing of disease-causing mutations has obvious attractions for the treatment of genetic disorders if the many practical obstacles to the technique can be overcome. One promising line of research centres on the development of zinc finger nucleases (ZFNs) produced by fusing an engineered zinc finger DNA-binding domain to an endonuclease. These artificial enzymes induce efficient gene correction in cultured cells. Li et al. now report that zinc finger nucleases induce double-strand breaks in specifically selected locations on the genome and stimulate genome editing at a clinically meaningful level in vivo. In a proof-of-principle experiment, ZFNs delivered to the liver in a mouse model of haemophilia B achieved a level of gene replacement that was sufficient to correct the clotting defect, and the effect persisted following liver regeneration. Editing of the human genome to correct disease-causing mutations is a promising approach for the treatment of genetic disorders. Genome editing improves on
Zinc-fingers play crucial roles in regulating gene expression and mediating protein-protein interactions. In this article, two different proteins (Sp1f2 and FSD-1) are investigated using the Gaussian network model and anisotropy elastic network model. By using these simple coarse-grained methods, we analyze the structural stabilization and establish the unfolding pathway of the two different proteins, in good agreement with related experimental and molecular dynamics simulation data. From the analysis, it is also found that the folding process of the zinc-finger motif is predominated by several factors. Both the zinc ion and C-terminal loop affect the folding pathway of the zinc-finger motif. Knowledge about the stability and folding behavior of zinc-fingers may help in understanding the folding mechanisms of the zinc-finger motif and in designing new zinc-fingers. Meanwhile, these simple coarse-grained analyses can be used as a general and quick method for mechanistic studies of metalloproteins.
foxP2, a forkhead-domain transcription factor, is critical for speech and language development in humans, but its role in the establishment of CNS connectivity is unclear. While in vitro studies have identified axon guidance molecules as targets of foxP2 regulation, and cell culture assays suggest a role for foxP2 in neurite outgrowth, in vivo studies have been lacking regarding a role for foxP2 in axon pathfinding. We used a modified zinc finger nuclease methodology to generate mutations in the zebrafish foxP2 gene. Using PCR-based high resolution melt curve analysis (HRMA) of G0 founder animals, we screened and identified three mutants carrying nonsense mutations in the 2nd coding exon: a 17 base-pair (bp) deletion, an 8bp deletion, and a 4bp insertion. Sequence analysis of cDNA confirmed that these were frameshift mutations with predicted early protein truncations. Homozygous mutant fish were viable and fertile, with unchanged body morphology, and no apparent differences in CNS apoptosis,
Bind-Predict is resource of database and software tools for identifying zinc finger protein binding motifs in mammalian genomes. The bind-predict has a user friendly interface tool named as Bind-predictdB and a database named as Bind-predictdB that are used to predict zinc finger binding sites in the user given input DNA sequence. Citation: Muthukumaran J, Jayakanthan M, Chandrasekar S, Mathur P.P. Bind-Predict: An algorithm for identifying zinc finger binding motifs in DNA sequences. J.Comp. Biol. Bioinfo. Res. 2011, 3(7): 91-102. [Journal], [PDF] ...
Nine KOX zinc finger genes were localized on four human chromosomes by in situ hybridization of cDNA probes to metaphase chromosomes. KOX1 (ZNF10), KOX11 (ZNF18), and KOX12 (ZNF19) were mapped to chro
TY - JOUR. T1 - A proteomic approach identifies SAFB-like transcription modulator (SLTM) as a bidirectional regulator of GLI family zinc finger transcription factors. AU - Zhang, Zilai. AU - Zhan, Xiaoming. AU - Kim, Bongwoo. AU - Wu, Jiang. PY - 2019/1/1. Y1 - 2019/1/1. N2 - In Sonic hedgehog (SHH) signaling, GLI family zinc finger (GLI)-mediated diverse gene transcription outcomes are strictly regulated and are important for SHH function in both development and disease. However, how the GLI factors differentially regulate transcription in response to variable SHH activities is incompletely understood. Here, using a newly generated, tagged Gli3 knock-in mouse (Gli3TAP), we performed proteomic analyses and identified the chromatin-associated SAFB-like transcription modulator (SLTM) as a GLI-interacting protein that context-dependently regulates GLI activities. Using immunoprecipitation and immunoblotting, RT-quantitative PCR, and ChIP assays, we show that SLTM interacts with all three GLI ...
GIW93P01] Yoichi Iida, Takeshi Masuda: "Quantification Analysis of Translation Initiation Signal Sequences in Vertebrate mRNAs" [GIW93P02] Koji Tajima: "Multiple Sequence Alignment using Parallel Genetic Algorithms" [GIW93P03] Tsuyoshi Yoshizawa, Masaki Fumoto, Tamio Yasukawa: "Prediction of Protein Conformations by a Spin Glass Model (I)" [GIW93P04] Fumiyoshi Sasagawa, Koji Tajima: "Toward Prediction of Multi-states Secondary Structures of Protein by Neural Network" [GIW93P05] Kotoko Nakata: "Sequence Analysis of Zinc Finger DNA-Binding Protein" [GIW93P06] Kazuhiro Iida, Hiroshi Mamitsuka: "Protein Sequence Motif Extraction with a Probabilistic Logic Neural Network: Motif Evaluation on a 3-D Structure" [GIW93P07] Koichi Niijima, Shinichi Shimozono: "Learning Algorithms of Three Layered Neural Networks for Sequence Classification" [GIW93P08] Hidetoshi Tanaka, Kentaro Onizuka, Kiyoshi Asai: "Classification of Proteins via Successive State Splitting Algorithm of Hidden Markov Network" [GIW93P09] ...
Ulnar polydactyl (left) and radial polydactyl (right). Do you know that famous Bollywood superstar Hritik Roshan has six fingers in one of his hand? Polydactyl is the terminology used to … ...
Human nucleoprotein 95 (NP95) is a member of a subfamily of RING-finger type E3 ubiquitin ligases and is encoded by the UHRF1 gene in humans. NP95 binds specifically to DNA and recruits a histone deacetylase to regulate gene expression. NP95 expression peaks at late G1 phase and continues during G2 and M phases of the cell cycle. It plays a major role in the G1/S transition by regulating topoisomerase II alpha and retinoblastoma (Rb) gene expression. NP95 also functions in the p53-dependent response to DNA damage, and its expression is upregulated in lymphomas induced by radiation. NP95 is also known as ubiquitin-like with PHD and ring finger domains 1 (UHRF1), ubiquitin-like PHD and RING finger domain-containing protein 1, RING finger protein 106 (RNF106), inverted CCAAT box-binding protein of 90 kDa (ICBP90), nuclear zinc finger protein Np95, E3 ubiquitin-protein ligase UHRF1, hUHRF1, hNP95, HuNp95, and FLJ21925.. ...
Human nucleoprotein 95 (NP95) is a member of a subfamily of RING-finger type E3 ubiquitin ligases and is encoded by the UHRF1 gene in humans. NP95 binds specifically to DNA and recruits a histone deacetylase to regulate gene expression. NP95 expression peaks at late G1 phase and continues during G2 and M phases of the cell cycle. It plays a major role in the G1/S transition by regulating topoisomerase II alpha and retinoblastoma (Rb) gene expression. NP95 also functions in the p53-dependent response to DNA damage, and its expression is upregulated in lymphomas induced by radiation. NP95 is also known as ubiquitin-like with PHD and ring finger domains 1 (UHRF1), ubiquitin-like PHD and RING finger domain-containing protein 1, RING finger protein 106 (RNF106), inverted CCAAT box-binding protein of 90 kDa (ICBP90), nuclear zinc finger protein Np95, E3 ubiquitin-protein ligase UHRF1, hUHRF1, hNP95, HuNp95, and FLJ21925.. ...
Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes. May regulate the expression of proteins involved in extracellular matrix development and maintenance, including fibrillar collagens, such as COL4A1 and COL11A1, connective tissue components, such as HAPLN1, and molecules regulating cell migration and adhesion, including EDIL3 and TGFB2. May cause G2/M arrest and apoptosis in cancer cells.
TY - JOUR. T1 - The zinc finger gene ZIC2 has features of an oncogene and its overexpression correlates strongly with the clinical course of epithelial ovarian cancer. AU - Marchini, Sergio. AU - Poynor, Elizabeth. AU - Barakat, Richard R.. AU - Clivio, Luca. AU - Cinquini, Michela. AU - Fruscio, Robert. AU - Porcu, Luca. AU - Bussani, Cecilia. AU - DIncalci, Maurizio. AU - Erba, Eugenio. AU - Romano, Michela. AU - Cattoretti, Giorgio. AU - Katsaros, Dionyssios. AU - Koff, Andrew. AU - Luzzatto, Lucio. PY - 2012/8/15. Y1 - 2012/8/15. N2 - Purpose: Epithelial ovarian tumors (EOT) are among the most lethal of malignancies in women.Wehave previously identified ZIC2 as expressed at a higher level in samples of a malignant form (MAL) of EOT than in samples of a form with low malignant potential (LMP). We have now investigated the role of ZIC2 in driving tumor growth and its association with clinical outcomes. Experimental Design: ZIC2 expression levels were analyzed in two independent tumor tissue ...
A zinc finger transposase is an engineered protein derived from a zinc finger DNA binding protein and a transposase. A transposase is an enzyme that reacts with DNA at specific sites and then clips that DNA region out of the source DNA forming a "transposome". This DNA/protein complex is highly reactive towards other DNAs. It reacts by inserting the DNA sequence mostly randomly into the target DNA. Zinc Finger proteins (ZF) are DNA binding proteins. The special thing about them is that 1) the ZFs bind long sequences of DNA, long enough that it might be unique in a eukaryotic genome, and 2) zinc finger proteins that bind to most sequences can be generated somewhat easily. By fusing ZFs to transposase, you can recruit the transposome to a specific site in the genome and thereby bias the insertion site of a transposome into a cells genome. You should read the following papers ...
Kim, Y. S., Kim, J. M., Jung, D. L., Kang, J. E., Lee, S., Kim, J. S., Seol, W., Shin, H. C., Kwon, H. S., Van Lint, C., Hernandez, N., Hur, M. W. (2005) Artificial zinc finger fusions targeting Sp1-binding sites and the trans-activator-responsive element potently repress transcription and replication of HIV-1. Journal of Biological Chemistry, 280 (22). pp. 21545-21552. ISSN 0021-9258 Kumar, A., Bhandari, A., Sinha, R., Sardar, P., Goyal, P., Goswami, C., Grapputo, A. (2012) Molecular Phylogeny of OVOL Genes Illustrates a Conserved C2H2 Zinc Finger Domain Coupled by Hypervariable Unstructured Regions. PLoS ONE, 7 (6). e39399. ISSN 1932-6203 ...
This entry represents B-box-type zinc finger domains, which are around 40 residues in length. B-box zinc fingers can be divided into two groups, where types 1 and 2 B-box domains differ in their consensus sequence and in the spacing of the 7-8 zinc-binding residues. Several proteins contain both types 1 and 2 B-boxes, suggesting some level of cooperativity between these two domains. B-box domains are found in over 1500 proteins from a variety of organisms. They are found in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). TRIM proteins contain a type 2 B-box domain, and may also contain a type 1 B-box. In proteins that do not contain RING or coiled-coil domains, the B-box domain is primarily type 2. Many type 2 B-box proteins are involved in ubiquitinylation. Proteins containing a B-box zinc finger domain include transcription factors, ...