A 100-kD HeLa cell octamer binding protein (OBP100) interacts differently with two separate octamer-related sequences within the SV40 enhancer.

Sturm, Richard A.; Baumruker, Thomas; Franza, B. R.; Herr, Winship

doi:10.1101/gad.1.10.1147

Cited by 239 publications

(140 citation statements)

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“…The restriction fragment probes for gel mobility-shift assays or immunoselection controls were 3'-end '2P-labelled HindIII-EcoRI digests of pUCl19H2B-box' (H2B wild-type octamer-containing fragment, H2B wt; Baumruker et al, 1988), pUC119B20wt' (SV40 site-I Octa-1 probc, SV40 Octa 1) and pUC119B20dpm8' (in which t a o positions of the SV40 site-I Octa-1 probe had been mutated to destroy Oct-1 binding, SV40 Octa 1 dpm8; , BamHI-PvuII digest of pUCll8AO (containing both SV40 octamer-binding sites Octa 1 and Octa 2; Sturm et al, 1987) and HindIIIPstI digest of pp6xB20 (containing six copies of the SV40 enhancer Octa-1 site; Ondek et al, 1988).…”

Section: Oligonucleotides Probes and Competitor Dna Fragmentsmentioning

confidence: 99%

“…HeLa heparin -agarose-fractionated nuclear extract (Sturm et al, 1987), an unfractionated HeLa total nuclear extract (see above) or a mouse brain total nuclear extract was initially incubated with 1 pg poly(d1-dC) . poly(d1-dC) in 12 mM Hepes, pH 7.9, 12% (by vol.)…”

Section: Electrophoretic Mobility-shift Assaysmentioning

confidence: 99%

“…This suggested that the overall affinity of Oct-1 for a sequence represents the aggregate of many specific base interactions though the indirect effect that base modification has on helix geometry was considered (Baumruker et al, 1988). Moreover, significant nucleotide and backbone contacts of full length Oct-1 or its POU domain have been shown to extend to the 5' side of the octamer motif (Sturm et al, 1987;Baumruker et al, 1988;Pruijn et al, 1988;Verrijzer et al, 1990b), suggesting that bases 5' of the octamer are also determinants of affinity and specificity.…”

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confidence: 99%

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Broad binding‐site specificity and affinity properties of octamer 1 and brain octamer‐binding proteins

Bendall

Sturm

Danoy

et al. 1993

European Journal of Biochemistry

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The ubiquitous Pit‐1‐Oct‐1‐Unc‐1 (POU)‐domain protein octamer 1 (Oct‐1) has been observed to bind specifically to a number of degenerate and dissimilar sequences. We have used antibodies directed against a C‐terminal Oct‐1 peptide to immunoselect binding sequences for HeLa cell Oct‐1 from random‐sequence oligonucleotides and we describe the isolation of binding sequences of considerable heterogeneity. Although our consensus alignment indicated a 9‐bp TATGCAAAT motif with AT‐rich flanking sequences, this binding motif is not immediately obvious in the population of sequences and no clone actually contained this sequence. Screening these Oct‐1‐binding sequences with a mouse whole‐brain extract demonstrated that the neuronal octamer‐binding proteins exhibit similar but distinct DNA sequence specificities. Unlike the reported selection of binding sequences for other transcription factors, the dependence of Oct‐1‐binding affinity upon sequence did not correspond tightly to the degree of conservation at particular positions of the consensus sequence. Our results suggest that either base‐specific hydrogen bonding is not the only major determinant of binding affinity and specificity, or that Oct‐1 binding to some sequences is mechanistically different from its binding to an octamer. These results exemplify the potential to overlook binding sites for some factors by searching gene sequences with a consensus nucleotide sequence.

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Section: Oligonucleotides Probes and Competitor Dna Fragmentsmentioning

confidence: 99%

Section: Electrophoretic Mobility-shift Assaysmentioning

confidence: 99%

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confidence: 99%

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Broad binding‐site specificity and affinity properties of octamer 1 and brain octamer‐binding proteins

Bendall

Sturm

Danoy

et al. 1993

European Journal of Biochemistry

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“…The sequence of MBP-1 does not contain any known DNA-binding motifs such as a zinc finger structure (25,43), leucine zipper (32), POU-specific regions (11,15,(64)(65)(66), or homeoboxes (33,40,42 Several groups have investigated the sequence requirement for initiation at the P1 and P2 start sites of the human c-myc gene (10,19,37,48,59). Sequences between -60 and -37 relative to the human c-myc P1 start site are essential for its activity in microinjected Xenopus laevis oocytes (48).…”

Section: Tcccctgtaccgccacatcgcgtacttggctggcaacttcgaagtcatcctgccagtcccmentioning

confidence: 99%

Cloning and characterization of a human c-myc promoter-binding protein.

Ray¹,

Miller²

1991

Mol. Cell. Biol.

107

128

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A human cDNA clone encoding a c-myc promoter-binding protein was detected by screening a HeLa cell k phage expression cDNA library. The library was screened by using an XhoI-NaeI human c-myc P2 promoter fragment as a probe. The recombinant phage encoded a fusion protein, myc-binding protein 1 (MBP-1), which had an apparent molecular size of 40 kDa. A corresponding protein with a molecular size of 35 kDa was present in a HeLa cell extract. Sequence analysis of the cloned gene reveals an open reading frame of 1,038 bp with a 3' untranslated region of 378 bp. The predicted protein sequence contains a proline-rich region in the amino terminus but does not demonstrate a known DNA-binding domain. DNase I footprint analysis demonstrates that MBP-1 binds to the sequence just 5' of the TATA box sequence of the human c-myc P2 promoter. MBP-1 cDNA hybridizes to a 1.4-kb mRNA from HeLa and HL-60 cells, indicating that the cDNA insert (1,416 bp) is a full-length clone. Coexpression of the MBP-1 protein represses transcription from the human c-myc promoter, suggesting that MBP-1 may act as a negative regulatory factor for the human c-myc gene.

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“…Several proteins that specifically bind the octamer sequence have been identified in nuclear extracts from mammalian cells. One such protein, termed octamer transcription factor (OTF-1; also called oct-1, NFA-1, OBP100, and NF III), is found in all tissue types tested; at least one other, termed OTF-2 (also called oct-2 and NFA-2), is found almost exclusively in lymphoid cells (23,32,37,45,46).…”

mentioning

confidence: 99%

The ubiquitous octamer-binding protein(s) is sufficient for transcription of immunoglobulin genes.

Johnson¹,

Carayannopoulos²,

Capra³

et al. 1990

Mol. Cell. Biol.

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All immunoglobulin genes contain a conserved octanucleotide promoter element, ATGCAAAT, which has been shown to be required for their normal B-cell-specific transcription. Proteins that bind this octamer have been purified, and cDNAs encoding octamer-binding proteins have been cloned. Some of these proteins (referred to as OTF-2) are lymphoid specific, whereas at least one other, and possibly more (referred to as OTF-1), is found ubiquitously in all cell types. The exact role of these different proteins in directing the tissue-specific expression of immunoglobulin genes is unclear. We have identified two human pre-B-cell lines that contain extremely low levels of OTF-2 yet still express high levels of steady-state immunoglobulin heavy-chain mRNA in vivo and efficiently transcribe an immunoglobulin gene in vitro. Addition of a highly enriched preparation of OTF-1 made from one of these pre-B cells or from HeLa cells specifically stimulated in vitro transcription of an immunoglobulin gene. Furthermore, OFT-1 appeared to have approximately the same transactivation ability as OTF-2 when normalized for binding activity. These results suggest that OTF-1, without OTF-2, is sufficient for transcription of immunoglobulin genes and that OTF-2 alone is not responsible for the B-cell-specific regulation of immunoglobulin gene expression.

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A 100-kD HeLa cell octamer binding protein (OBP100) interacts differently with two separate octamer-related sequences within the SV40 enhancer.

Cited by 239 publications

References 53 publications

Broad binding‐site specificity and affinity properties of octamer 1 and brain octamer‐binding proteins

Broad binding‐site specificity and affinity properties of octamer 1 and brain octamer‐binding proteins

Cloning and characterization of a human c-myc promoter-binding protein.

The ubiquitous octamer-binding protein(s) is sufficient for transcription of immunoglobulin genes.

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