A Xenopus zinc finger protein that specifically binds dsRNA and RNA-DNA hybrids

Finerty, P.J.; Bass, Brenda

doi:10.1006/jmbi.1997.1177

Cited by 43 publications

(53 citation statements)

References 57 publications

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“…It is estimated that zinc finger proteins may comprise 1% of all proteins encoded by the human genome (Hoovers et al 1992), and they represent 0.7% of the proteins encoded in the Caenorhabditis elegans genome (Clarke and Berg 1998). Although best known as sequence-specific DNA-binding motifs in many transcription factors, the C2H2 zinc fingers also can mediate binding of proteins to single- (Draper 1995) and doublestranded RNAs (Finerty andBass 1997, 1999), RNA-DNA hybrids (Shi and Berg 1995), and to other zinc finger proteins (Mackay and Crossley 1998). Zinc finger proteins of the C2H2 type have been implicated in many aspects of cellular RNA metabolism, including premRNA splicing (Larsson et al 1995;Davies et al 1998) and RNA storage (Joho et al 1990).…”

Section: The Rna-supplemented Two-hybrid System Can Be Used To Clone mentioning

confidence: 99%

A novel zinc finger protein is associated with U7 snRNP and interacts with the stem–loop binding protein in the histone pre-mRNP to stimulate 3′-end processing

Domiński¹,

Erkmann²,

Yang³

et al. 2002

Genes Dev.

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The stem-loop binding protein (SLBP) is the posttranscriptional regulator of histone mRNA in metazoan cells. SLBP binds histone pre-mRNAs and facilitates 3-end processing by promoting stable association of U7 snRNP with the pre-mRNA. To identify other factors involved in histone pre-mRNA processing, we used a modified yeast two-hybrid assay in which SLBP and its RNA target were coexpressed as bait. A novel zinc finger protein, hZFP100, which interacts with the SLBP/RNA complex but not with free SLBP, was cloned. The interaction requires regions of SLBP that are important for histone pre-mRNA processing. Antibodies to hZFP100 precipitate U7 snRNA, and expression of hZFP100 in Xenopus oocytes stimulates processing of histone pre-mRNA, showing that hZFP100 is a component of the processing machinery.

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Section: The Rna-supplemented Two-hybrid System Can Be Used To Clone mentioning

confidence: 99%

A novel zinc finger protein is associated with U7 snRNP and interacts with the stem–loop binding protein in the histone pre-mRNP to stimulate 3′-end processing

Domiński¹,

Erkmann²,

Yang³

et al. 2002

Genes Dev.

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“…on May 11, 2018. by guest www.bloodjournal.org From preferentially bind dsRNA in vitro. [41][42][43][44][45] Of interest, these 2 dsRNA-binding ZFPs also contain unusually long linker sequences (ie, 34-44 amino acids for dsRBP-Zfa and 54-77 amino acids for PAG608/Wig-1). 41,42,44 While the function of dsRBP-Zfa remains unknown, JAZ and PAG608/Wig-1 can induce apoptosis when ectopically expressed in cells.…”

mentioning

confidence: 99%

“…[41][42][43][44][45] Of interest, these 2 dsRNA-binding ZFPs also contain unusually long linker sequences (ie, 34-44 amino acids for dsRBP-Zfa and 54-77 amino acids for PAG608/Wig-1). 41,42,44 While the function of dsRBP-Zfa remains unknown, JAZ and PAG608/Wig-1 can induce apoptosis when ectopically expressed in cells. 32,41,46 In addition, PAG608/Wig-1 was shown to inhibit cell growth in a colony-formation assay, but the mechanism is not known.…”

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confidence: 99%

JAZ mediates G1 cell-cycle arrest and apoptosis by positively regulating p53 transcriptional activity

Yang

et al. 2006

Blood

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We previously identified JAZ as a novel zinc finger (ZF) protein by screening a murine interleukin-3 (IL-3)-dependent NFS/N1.H7 myeloid cell cDNA library. JAZ is a member of a new class of ZFPs that is evolutionarily conserved and preferentially binds to dsRNA, but its function was unknown. Now, we report that the stress of IL-3 growth factor withdrawal upregulates JAZ expression in hematopoietic cells in association with p53 activation and induction of cell death. Biochemical analysis reveals that JAZ associates with p53 to stimulate its transcriptional activity in p53-expressing cells, but not in p53-null cells unless complemented with p53. JAZ functions to mediate G 1 cell-cycle arrest followed by apoptosis in a p53-dependent mechanism that is associated with up-regulation of p21 and BAX, dephosphorylation of Rb, and repression of cyclin A. Of importance, siRNA "knockdown" of endogenous JAZ inhibits p53 transcriptional activity, decreases the G 1 /G 0 population, and attenuates stress-induced cell death. While JAZ directly binds p53 in vitro in a mechanism requiring p53's Cterminal regulatory domain but independent of dsRNA, the dsRNA-binding ZF domains are required for JAZ's stimulatory role of p53 in vivo by dictating its nuclear localization. Thus, JAZ is a novel negative regulator of cell growth by positively regulating p53. IntroductionThe p53 tumor-suppressor gene is the most frequent target of genetic inactivation in human cancer. 1 p53 is a homotetrameric transcription factor with several distinct domains for its function and regulation. 2,3 Most of the tumor-associated mutations in p53 occur in the core DNA-binding domain and disrupt the DNAbinding/transactivational activity of p53. 1 p53 transactivationdeficient mice develop spontaneous tumors, indicating that the transcriptional activity of p53 is essential for its potent tumorsuppressor function. 4,5 p53 can transactivate a number of genes containing p53-response elements including p21 and BAX, which play key roles in p53-mediated growth arrest and apoptosis. 1,6 In addition, p53 can function extranuclearly by directly inhibiting Bcl2/Bcl XL or activating BAX at the mitochondria to induce apoptosis. [7][8][9] p53 acts as a central negative regulator of cell growth by integrating genotoxic stress signals. 1 However, p53 is also reported to respond to nongenotoxic stresses, but the mechanism(s) is not well understood. 10 In response to DNA damage, growth factor depletion, chromosomal aberrations, telomere erosion, oncogene activation, and hypoxia, p53 is activated to induce growth arrest, differentiation, or apoptosis. 1,10 p53 has also been reported to be necessary for efficient hematopoietic growth factor withdrawalinduced apoptosis. [11][12][13][14][15][16] Furthermore, regulation of p53 is central to normal cell growth and tumor suppression, but the mechanism by which p53 is regulated is complex and still not fully understood. 17,18 However, it is clear that interaction with cellular proteins plays an important role in p53 regulation. 17 For ex...

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“…In vitro isolation of oligonucleotides containing a ZNF300 binding site through the random oligonucleotide selection strategy The C 2 H 2 -type zinc finger proteins usually function as transcription factors and bind to DNA, RNA and RNA-DNA hybrids, but mostly interact with DNA [12][13][14]. ZNF300 is a nuclear protein [4], and thus may be a sequence-specific DNAbinding protein.…”

Section: Resultsmentioning

confidence: 99%

Identification of the DNA binding element of the human ZNF300 protein

Qiu

Lü

Gao

et al. 2008

Cellular and Molecular Biology Letters

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The human ZNF300 gene is a member of the KRAB/C2H2 zinc finger gene family, the members of which are known to be involved in various developmental and pathological processes. Here, we show that the ZNF300 gene encodes a 68-kDa nuclear protein that binds DNA in a sequence-specific manner. The ZNF300 DNA binding site, C(t/a)GGGGG(c/g)G, was defined via a random oligonucleotide selection assay, and the DNA binding site was further confirmed by electrophoretic mobility shift assays. A potential ZNF300 binding site was found in the promoter region of the human IL-2Rβ gene. The results of electrophoretic mobility shift assays indicated that ZNF300 bound to the ZNF300 binding site in the IL-2Rβ promoter in vitro. Transient co-transfection assays showed that ZNF300 could activate the IL-2Rβ promoter, and that the activation was abrogated by the mutation of residues in the ZNF300 binding site. Identifying the DNA binding site and characterizing the transcriptional regulation property of ZNF300 would provide critical insights into its potential as a transcriptional regulator.

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A Xenopus zinc finger protein that specifically binds dsRNA and RNA-DNA hybrids

Cited by 43 publications

References 57 publications

A novel zinc finger protein is associated with U7 snRNP and interacts with the stem–loop binding protein in the histone pre-mRNP to stimulate 3′-end processing

A novel zinc finger protein is associated with U7 snRNP and interacts with the stem–loop binding protein in the histone pre-mRNP to stimulate 3′-end processing

JAZ mediates G1 cell-cycle arrest and apoptosis by positively regulating p53 transcriptional activity

Identification of the DNA binding element of the human ZNF300 protein

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