Identification, nuclear localization, and DNA-binding activity of the zinc finger protein encoded by the Evi-1 myeloid transforming gene.

Activation of the Evi-1 zinc finger gene is a common event associated with transformation of murine myeloid leukemias. To characterize the gene product, we developed antisera against various protein domains. These antisera primarily detected a 145-kilodalton nuclear protein that bound double-stranded DNA. Binding was inhibited by chelating agents and partially restored by zinc ions.

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The rat cytomegalovirus homologue of parvoviral rep genes, r127, encodes a nuclear protein with single- and double-stranded DNA-binding activity that is dispensable for virus replication

Journal of General Virology ◽

10.1099/vir.0.79864-0 ◽

2004 ◽

Vol 85 (7) ◽

pp. 2001-2013 ◽

Cited By ~ 6

Author(s):

Koen W. R. van Cleef ◽

Wendy M. A. Scaf ◽

Karen Maes ◽

Suzanne J. F. Kaptein ◽

Erik Beuken ◽

...

Keyword(s):

Dna Binding ◽

Virus Replication ◽

Deletion Mutant ◽

Nuclear Protein ◽

Human Herpesvirus ◽

Binding Activity ◽

Dna Binding Activity ◽

Double Stranded Dna

An intriguing feature of the rat cytomegalovirus (RCMV) genome is open reading frame (ORF) r127, which shows similarity to the rep genes of parvoviruses as well as the U94 genes of human herpesvirus type 6A (HHV-6A) and 6B (HHV-6B). Counterparts of these genes have not been found in other herpesviruses. Here, it is shown that the r127 gene is transcribed during the early and late phases of virus replication in vitro as an unspliced 1·1 kb transcript containing the complete r127 ORF. Transcripts of r127 were also detected in various organs of RCMV-infected rats at 1 week post-infection (p.i.), but only in the salivary gland at 4 months p.i. Using rabbit polyclonal antibodies raised against the r127-encoded protein (pr127), pr127 was found to be expressed as early as 12 h p.i. within the nuclei of RCMV-infected cells in vitro. Expression of pr127 was also observed within the nuclei of cells in various organs of RCMV-infected rats at 3 weeks p.i. Moreover, pr127 was demonstrated to bind single- as well as double-stranded DNA. Finally, an RCMV r127 deletion mutant (RCMVΔr127) was generated, in which the r127 ORF was disrupted. This deletion mutant, however, was shown to replicate with a similar efficiency as wild-type RCMV (wt RCMV), both in vitro and in vivo. Taken together, it is concluded that the RCMV r127 gene encodes a nuclear protein with single- and double-stranded DNA-binding activity that is dispensable for virus replication, not only in vitro, but also during the acute phase of infection in vivo.

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Dual Histone Methyl Reader ZCWPW1 Facilitates Repair of Meiotic Double Strand Breaks

10.1101/821603 ◽

2019 ◽

Cited By ~ 4

Author(s):

Mohamed Mahgoub ◽

Jacob Paiano ◽

Melania Bruno ◽

Wei Wu ◽

Sarath Pathuri ◽

...

Keyword(s):

Dna Binding ◽

Zinc Finger ◽

Histone Methylation ◽

Zinc Finger Protein ◽

Genetic Recombination ◽

Binding Activity ◽

Double Strand Breaks ◽

Gene Promoters ◽

Strand Breaks ◽

Dna Binding Activity

SummaryMeiotic crossovers result from homology-directed repair of double strand breaks (DSBs). Unlike yeast and plants, where DSBs are generated near gene promoters, in many vertebrates, DSBs are enriched at hotspots determined by the DNA binding activity of the rapidly evolving zinc finger array of PRDM9 (PR domain zinc finger protein 9). PRDM9 subsequently catalyzes tri-methylation of lysine 4 and lysine 36 of Histone H3 in nearby nucleosomes. Here, we identify the dual histone methylation reader ZCWPW1, which is tightly co-expressed during spermatogenesis with Prdm9 and co-evolved with Prdm9 in vertebrates, as an essential meiotic recombination factor required for efficient synapsis and repair of PRDM9-dependent DSBs. In sum, our results indicate that the evolution of a dual histone methylation writer/reader system in vertebrates facilitated a shift in genetic recombination away from a static pattern near genes towards a flexible pattern controlled by the rapidly evolving DNA binding activity of PRDM9.

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Faculty Opinions recommendation of Embryonic neural inducing factor churchill is not a DNA-binding zinc finger protein: solution structure reveals a solvent-exposed beta-sheet and zinc binuclear cluster.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1100091.556249 ◽

2008 ◽

Author(s):

Thomas Friedman

Keyword(s):

Dna Binding ◽

Zinc Finger ◽

Solution Structure ◽

Zinc Finger Protein ◽

Beta Sheet ◽

Protein Solution ◽

Binuclear Cluster ◽

Finger Protein ◽

Zinc Binuclear Cluster

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DNA Binding by the Methanothermobacter thermautotrophicus Cdc6 Protein Is Inhibited by the Minichromosome Maintenance Helicase

Journal of Bacteriology ◽

10.1128/jb.00168-06 ◽

2006 ◽

Vol 188 (12) ◽

pp. 4577-4580 ◽

Cited By ~ 14

Author(s):

Rajesh Kasiviswanathan ◽

Jae-Ho Shin ◽

Zvi Kelman

Keyword(s):

Dna Binding ◽

Binding Activity ◽

Minichromosome Maintenance ◽

Single Stranded Dna ◽

Mutant Proteins ◽

Dna Binding Activity ◽

Double Stranded Dna ◽

Mcm Helicase ◽

Methanothermobacter Thermautotrophicus

ABSTRACT The Cdc6 proteins from the archaeon Methanothermobacter thermautotrophicus were previously shown to bind double-stranded DNA. It is shown here that the proteins also bind single-stranded DNA. Using minichromosome maintenance (MCM) helicase mutant proteins unable to bind DNA, it was found that the interaction of MCM with Cdc6 inhibits the DNA binding activity of Cdc6.

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The Human Monocytic Leukemia Zinc Finger Histone Acetyltransferase Domain Contains DNA-binding Activity Implicated in Chromatin Targeting

Journal of Biological Chemistry ◽

10.1074/jbc.m705812200 ◽

2007 ◽

Vol 282 (50) ◽

pp. 36603-36613 ◽

Cited By ~ 30

Author(s):

Marc A. Holbert ◽

Timothy Sikorski ◽

Juliana Carten ◽

Danielle Snowflack ◽

Santosh Hodawadekar ◽

...

Keyword(s):

Dna Binding ◽

Zinc Finger ◽

Histone Acetyltransferase ◽

Binding Activity ◽

Monocytic Leukemia ◽

Dna Binding Activity ◽

Human Monocytic Leukemia ◽

Acetyltransferase Domain

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Characterization of the DNA Binding Activity of the ZFY Zinc Finger Domain

Biochemistry ◽

10.1021/bi9018626 ◽

2010 ◽

Vol 49 (4) ◽

pp. 679-686 ◽

Cited By ~ 4

Author(s):

Jennifer Grants ◽

Erin Flanagan ◽

Andrea Yee ◽

Paul J. Romaniuk

Keyword(s):

Dna Binding ◽

Zinc Finger ◽

Binding Activity ◽

Zinc Finger Domain ◽

Dna Binding Activity

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Toward rules relating zinc finger protein sequences and DNA binding site preferences.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.89.16.7345 ◽

1992 ◽

Vol 89 (16) ◽

pp. 7345-7349 ◽

Cited By ~ 144

Author(s):

J. R. Desjarlais ◽

J. M. Berg

Keyword(s):

Dna Binding ◽

Binding Site ◽

Zinc Finger ◽

Zinc Finger Protein ◽

Protein Sequences ◽

Site Preferences ◽

Finger Protein ◽

Dna Binding Site

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Single amino acid exchanges in separate domains of the Drosophila serendipity delta zinc finger protein cause embryonic and sex biased lethality.

Genetics ◽

10.1093/genetics/131.4.905 ◽

1992 ◽

Vol 131 (4) ◽

pp. 905-916 ◽

Cited By ~ 2

Author(s):

M Crozatier ◽

K Kongsuwan ◽

P Ferrer ◽

J R Merriam ◽

J A Lengyel ◽

...

Keyword(s):

Amino Acid ◽

Dna Binding ◽

Zinc Finger ◽

Zinc Finger Protein ◽

Essential Gene ◽

Larval Instar ◽

Single Amino Acid ◽

Isolation And Characterization ◽

Finger Protein

Abstract The Drosophila serendipity (sry) delta (delta) zinc finger protein is a sequence-specific DNA binding protein, maternally inherited by the embryo and present in nuclei of transcriptionally active cells throughout fly development. We report here the isolation and characterization of four ethyl methanesulfate-induced zygotic lethal mutations of different strengths in the sry delta gene. For the stronger allele, all of the lethality occurs during late embryogenesis or the first larval instar. In the cases of the three weaker alleles, most of the lethality occurs during pupation; moreover, those adult escapers that emerge are sterile males lacking partially or completely in spermatozoa bundles. Genetic analysis of sry delta thus indicates that it is an essential gene, whose continued expression throughout the life cycle, notably during embryogenesis and pupal stage, is required for viability. Phenotypic analysis of sry delta hemizygote escaper males further suggests that sry delta may be involved in regulation of two different sets of genes: genes required for viability and genes involved in gonadal development. All four sry delta alleles are fully rescued by a wild-type copy of sry delta, but not by an additional copy of the sry beta gene, reinforcing the view that, although structurally related, these two genes exert distinct functions. Molecular characterization of the four sry delta mutations revealed that these mutations correspond to single amino acid replacements in the sry delta protein. Three of these replacements map to the same (third out of seven) zinc finger in the carboxy-terminal DNA binding domain; interestingly, none affects the zinc finger consensus residues. The fourth mutation is located in the NH2-proximal part of the protein, in a domain proposed to be involved in specific protein-protein interactions.

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