High-resolution localization of 69 potential human zinc finger protein genes: A number are clustered

Hoovers, J. M. N.; Mannens, Marcel; Roshan, John; Bliek, Jet; Heyningen, Veronica van; Porteous, David J.; Leschot, N. J.; Westerveld, A.; Little, Peter

doi:10.1016/0888-7543(92)90372-y

Cited by 125 publications

(78 citation statements)

References 34 publications

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“…It has been estimated that up to 1% of all genes in the human genome may encode proteins with zinc finger domains (12). Although the structure of a large number of these molecules has been characterized (13,14), conserved elements outside of the finger repeats are rare (15,16).…”

mentioning

confidence: 99%

Molecular Cloning of a Zinc Finger Autoantigen Transiently Associated with Interphase Nucleolus and Mitotic Centromeres and Midbodies

Bolı́var

Diaz

Iglesias

et al. 1999

Journal of Biological Chemistry

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We have cloned a novel human autoimmune antigen in a patient suffering from rheumatoid arthritis with high levels of antibodies to the nucleolus organizer regions. Initially the human autoimmune serum was used to select a cDNA of 317 amino acids from a hamster expression library. Using the hamster DNA as a probe, we isolated the human homologous cDNA of 320 amino acids. Human and hamster polypeptides share a 95% amino acid homology. The deduced 36-kDa protein contains a putative amino-terminal NLS signal, nine cysteine-X-X-cysteine motifs highly conserved, and a carboxyl-terminal poly acidic region. Several homologous expressed sequence tags have been identified in data bases suggesting that orthologous proteins are present throughout evolution from worms to humans. A Drosophila expressed sequence tag was further completely sequenced for a full-length protein with 60% amino acid identity to the human homologue. Northern blot analysis revealed that this novel protein is widely distributed in human tissues with significantly higher expression levels in heart and skeletal muscle. Specific antibodies to the recombinant protein and transfection experiments demonstrated by immunofluorescence the localization of the protein predominantly but not exclusively to the nucleolus of interphase mammalian cells. In actinomycin D-treated cells the protein remains associated with the nucleolus but is not segregated, like other ribosomal factors such as upstream binding factor. In mitosis the protein was found to be associated with centromeres and concentrated at the midbody in cytokinesis. Transient distribution of this evolutionarily conserved zinc finger nucleolar autoantigen to the mitotic centromeres may provide the means for several aspects of cell cycle control and transcriptional regulation.

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confidence: 99%

Molecular Cloning of a Zinc Finger Autoantigen Transiently Associated with Interphase Nucleolus and Mitotic Centromeres and Midbodies

Bolı́var

Diaz

Iglesias

et al. 1999

Journal of Biological Chemistry

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“…When compared with ideograms in a similar state of contraction, this method gives a very accurate chromosomal assignment. 31 …”

Section: Physical Mappingmentioning

confidence: 99%

An integrated map of chromosome 18 CAG trinucleotide repeat loci

et al. 1999

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Expansions of trinucleotide CAG repeats have been demonstrated in at least eight neurodegenerative disorders, and suggested to occur in several others, including bipolar disorder and schizophrenia. Chromosome 18 loci have been implicated in bipolar disorder pedigrees by linkage analysis. To address this putative link between chromosome 18 CAG trinucleotide repeats and neuropsychiatric illness, we have screened a chromosome 18 cosmid library (LL18NCO2 ² AD ² ) and identified 14 novel candidate loci. Characterisation of these loci involved repeat flank sequencing, estimation of polymorphism frequency and mapping using FISH as well as radiation hybrid panels. These mapped trinucleotide loci will be useful in the investigation of chromosome 18 in neurodegenerative or psychiatric conditions, and will serve to integrate physical and radiation hybrid maps of chromosome 18.

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“…Its nutritional importance can be illustrated by the large number of proteins that require zinc for their function. For example, there are over 300 known zinc metalloenzymes (1), and it has been estimated that as many as 1% of the genes in the human genome encode proteins with C 2 H 2 zinc finger motifs (2). In contrast, zinc excess can be toxic to cells so mechanisms of controlling intracellular zinc levels are critical to cell viability.…”

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confidence: 99%

“…3 This element is found in one or more copies in the promoter regions of Zap1 target genes. Experimental evidence (8) and computeraided motif analysis of Zap1 target gene promoters 2 have indicated that the sequence 5Ј-ACCTTNAAGGT-3Ј is the preferred recognition site for this protein. Determining how Zap1 recognizes and binds to this sequence is a critical issue in understanding how Zap1 functions as a transcriptional activator.…”

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confidence: 99%

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Mapping the DNA Binding Domain of the Zap1 Zinc-responsive Transcriptional Activator

Bird

Evans-Galea

Blankman

et al. 2000

Journal of Biological Chemistry

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The Zap1 transcriptional activator of Saccharomyces cerevisiae plays a major role in zinc homeostasis by inducing the expression of several genes under zinc-limited growth conditions. This activation of gene expression is mediated by binding of the protein to one or more zinc-responsive elements present in the promoters of its target genes. To better understand how Zap1 functions, we mapped its DNA binding domain using a combined in vivo and in vitro approach. Our results show that the Zap1 DNA binding domain maps to the carboxyl-terminal 194 amino acids of the protein; this region contains five of its seven potential zinc finger domains. Fusing this region to the Gal4 activation domain complemented a zap1⌬ mutation for low zinc growth and also conferred high level expression on a zinc-responsive element-lacZ reporter. In vitro, the purified 194-residue fragment bound to DNA with a high affinity (dissociation constant in the low nanomolar range) similar to that of longer fragments of Zap1. Furthermore, by deletion and sitedirected mutagenesis, we demonstrated that each of the five carboxyl-terminal zinc fingers are required for high affinity DNA binding.

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High-resolution localization of 69 potential human zinc finger protein genes: A number are clustered

Cited by 125 publications

References 34 publications

Molecular Cloning of a Zinc Finger Autoantigen Transiently Associated with Interphase Nucleolus and Mitotic Centromeres and Midbodies

Molecular Cloning of a Zinc Finger Autoantigen Transiently Associated with Interphase Nucleolus and Mitotic Centromeres and Midbodies

An integrated map of chromosome 18 CAG trinucleotide repeat loci

Mapping the DNA Binding Domain of the Zap1 Zinc-responsive Transcriptional Activator

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