A family of human CCAAT-box-binding proteins active in transcription and DNA replication: cloning and expression of multiple cDNAs

Santoro, Claudio; Mermod, Nicolas; Andrews, Philip C.; Tjian, Robert

doi:10.1038/334218a0

Cited by 737 publications

(536 citation statements)

References 51 publications

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“…What is the molecular mechanism by which the interaction between CTF1 and HOX11 might modulate the rate of cell proliferation? CTF1 acts as an ubiquitous transcription factor and directs expression of a variety of eukaryotic genes (Santoro et al, 1988). Although HOX11 has previously been shown to be capable of direct DNA binding and transactivation, our current data suggest a role for HOX11 in modulating CTF1 function.…”

Section: Discussioncontrasting

confidence: 56%

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HOX11 interacts with CTF1 and mediates hematopoietic precursor cell immortalization

et al. 1999

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HOX11 is a homeodomain-containing oncogenic transcription factor that immortalizes hematopoietic precursor cells. The mechanism by which HOX11 facilitates this initial step of leukemogenesis is, however, not well understood. We have used a DNA binding site selection assay to investigate cooperative DNA binding by HOX11 with other transcription factors. A consensus sequence was derived and identi®ed as the binding site for the CCAAT-box-binding transcription factors (CTF). HOX11 was shown to interact in vitro and in vivo with CTF1. Retrovirus-mediated transduction of an antisense CTF1 cDNA dramatically reduced the proliferative capacity of HOX11-immortalized hematopoietic precursor cells. CTF1 is, therefore, the ®rst HOX11 protein partner identi®ed that plays an important role in hematopoietic precursor cell immortalization.

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Section: Discussioncontrasting

confidence: 56%

“…The CTF1 cDNA in Bluescript SK + (Santoro et al, 1988) was digested with BamHI, blunted with the Klenow fragment and cloned, in the antisense orientation, into the MSCV retroviral vector (Hawley et al, 1994). Recombinant retroviruses were produced using the PA317 amphotropic packaging cell line.…”

Section: Retrovirus-mediated Gene Transductionmentioning

confidence: 99%

HOX11 interacts with CTF1 and mediates hematopoietic precursor cell immortalization

et al. 1999

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“…For example, in the lysis/lysogeny switch of bacteriophage λ, cro and repressor compete for related sites in the rightward operator 28 . In eukaryotes, a number of regulatory proteins have been shown to be members of protein families with related DNA-binding specificities [29][30][31][32][33][34][35][36][37] . In fact, a member of the nuclear hormone receptor family, thyroid hormone receptor, was recently shown to mediate negative effects on transcription from oestrogen-responsive DNA elements, apparently by competing with oestrogen receptor for binding to the elements 38 .…”

Section: Discussionmentioning

confidence: 99%

Activation and repression of transcription by homoeodomain-containing proteins that bind a common site

Jaynes

O’Farrell

1988

Nature

223

148

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The product of the fushi tarazu (ftz) gene is shown to be a site-dependent activator of transcription. In vitro-defined binding sites act as ftz-dependent enhancers in cultured cells. Another homoeodomain-containing protein, the engrailed gene product, competes for homoeodomainbinding sites and counteracts ftz activation.GENETIC analysis in Drosophila melanogaster has identified a group of regulatory genes that participate in embryonic pattern formation 1,2 . Many of these genes encode a 60 amino-acid sequence, the homoeodomain, that is highly conserved through evolution [3][4][5] . This domain contains a putative helix-turn-helix motif 6 such as that found in a number of bacterial regulators 7 , and possesses a sequence-specific DNA-binding activity 8,9 . Numerous regulatory interactions occur among homoeodomain-encoding genes during development. For example, a combination of segmentation and homoeotic gene products, many of which contain homoeodomains 1 , specify the developmental fates of cells in striped patterns 10,11 . Furthermore, homoeodomain-containing proteins (homoeodomain proteins) regulate both each other 12 and downstream (`cytodifferentiation' 13 ) genes. Consequently, it has been attractive to think of homoeodomain proteins as direct regulators of transcription. Due to the complexity of cross-regulatory interactions however, mutations altering or eliminating one homoeodomain protein generally change the expression patterns of many other regulators, confounding efforts to distinguish direct from indirect regulation. Additionally, suspected target genes contain large cis-acting control regions that respond, directly or indirectly, to complex combinations of regulators [14][15][16][17] . As a result, identification of target genes directly regulated by homoeodomain proteins has been problematic.Previous studies have documented instances in which homoeodomain proteins control transcription. The enhancer activity of a DNA fragment from the ftz gene, a homoeodomaincontaining member of the pair-rule class of segmentation genes, suggested that the ftz gene product (ftz) activates its own expression in the embryo 18 . In a different approach a Drosophila tissue culture system was used to show that the Ultrabithorax (Ubx) gene product induces expression of its own promoter, and inhibits the Antennapedia (Antp) (P1) promoter (M. Krasnow and D. S. Hogness, personal communication, see ref. 19 for summary). In these cases however, the complexity of the regulatory circuitry and of the responding control regions leaves open the possibility that the homoeodomain proteins produce these transcriptional effects through intermediaries. To circumvent the complexities of natural target genes, we chose to use binding sites identified in vitro to build homoeodomain-responsive promoters. We find that ftz is a potent activator of transcription from these promoters in cultured cells.During sequential subdivision of the Drosophila embryo to produce segmentally repeating patterns, combinations of regulatory gene prod...

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“…Several lines of evidence, including direct comparison of proteins and immunological as well as sequence studies [18][19][20][21] indicate that NFI and NFIII are very closely related or identical to the transcription factors CTF (CCAAT-box binding factor) and OTFI (octamer-binding transcription factor), respectively. This indicates that adenovirus employs cellular transcription factors for optimal initiation of DNA replication, reinforcing the link between replication and transcription which has been observed for other eukaryotic DNA viruses [221.…”

Section: Introductionmentioning

confidence: 99%

Adenovirus DNA replication in vitro: Duplication of single-stranded DNA containing a panhandle structure

Leegwater

Rombouts

Vliet

1988

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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Adenovirus DNA replicates by displacement of one of the parental strands followed by duplication of the displaced parental single strand (complementary strand synthesis). Displacement synthesis has been performed in a reconstituted system composed of viral and cellular proteins, employing either the viral DNA-terminal protein complex as template or linearized plasmids containing the origin. Previously, evidence was obtained that in vivo complementary strand synthesis requires formation of a panhandle structure originating from hybridization of the inverted terminal repeats. To study the conditions for complementary strand synthesis in vitro, we have constructed an artificial panhandle molecule that contains a double-stranded inverted terminal repetition (ITR) region and a single-stranded loop derived from the left and right terminal Xma I fragments of Ad2. Such a molecule appeared to be an efficient template and could initiate by the same protein-priming mechanism as double-stranded DNA, employing the precursor terminal protein. The efficiency of both types of template was comparable. Like for replication of the duplex molecule initiation of panhandle replication was stimulated by nuclear factors I and III, proteins that bind to specific double-stranded regions of the ITR. The Ad DNA-binding protein is essential and the 39 kDa C-terminal domain of this protein that harbors the DNA-binding properties is sufficient for its function. These results support the hypothesis that panhandle formation is required for duplication of the displaced strand.

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A family of human CCAAT-box-binding proteins active in transcription and DNA replication: cloning and expression of multiple cDNAs

Cited by 737 publications

References 51 publications

HOX11 interacts with CTF1 and mediates hematopoietic precursor cell immortalization

HOX11 interacts with CTF1 and mediates hematopoietic precursor cell immortalization

Activation and repression of transcription by homoeodomain-containing proteins that bind a common site

Adenovirus DNA replication in vitro: Duplication of single-stranded DNA containing a panhandle structure

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