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Cloning and Characterization of a Human c- myc Promoter-Binding Protein

Ray, R, Miller, D M·1991·Molecular and Cellular Biology

Abstract

A human cDNA clone encoding a c-myc promoter-binding protein was detected by screening a HeLa cell lambda 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 repress 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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  • ENO1 is a multifunctional protein that promotes the Warburg effect as a classical glycolytic enzyme and also acts as a plasminogen receptor and DNA-binding protein.

    “ENO1 is a multifunctional protein that not only promotes the Warburg effect as a classical glycolytic enzyme but also acts as a plasminogen receptor and DNA-binding protein (Miles et al., 1991; Ray and Miller, 1991).”

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Metadata

Authors
Ray, R., & Miller, D. M.
Venue
Molecular and Cellular Biology
Published
1991-04
Volume
11
Issue
4
Pages
2154-2161
ISSN
  • 0270-7306
  • 1098-5549
Cited by
55
References
0
Language
en

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