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Novel nuclear matrix protein HET binds to and influences activity of the HSP27 promoter in human breast cancer cells by Steffi Oesterreich; Adrian V. Lee; Toby M. Sullivan; Shanti K. Samuel; James R. Davie; Suzanne A.W. Fuqua is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Since the small heat shock protein hsp27 enhances both growth and drug resistance in breast cancer cells, and is a bad prognostic factor in certain subsets of breast cancer patients, we have characterized the transcriptional regulation of hsp27, with the long-term goal of targeting its expression clinically. The majority of the promoter activity resides in the most proximal 200 bp. This region contains an imperfect estrogen response element (ERE) that is separated by a 13-bp spacer that contains a TATA box. Gel-shift analysis revealed the binding of a protein (termed HET for Hsp27-ERE-TATA-binding protein) to this region that was neither the estrogen receptor nor TATA-binding protein. We cloned a complete cDNA (2.9 kb) for HET from an MCF-7 cDNA library. To confirm the identity of the HET clone, we expressed a partial HET clone as a glutathione S-transferase fusion protein, and showed binding to the hsp27 promoter fragment in gel-retardation assays. The HET clone is almost identical to a recently published scaffold attachment factor (SAF-B) cloned from a HeLa cell cDNA library. Scaffold attachment factors are a subset of nuclear matrix proteins (NMP) that interact with matrix attac

Who reads Novel nuclear matrix protein HET binds to and influences activity of the HSP27 promoter in human breast cancer cells?

Author

Steffi Oesterreich; Adrian V. Lee; Toby M. Sullivan; Shanti K. Samuel; James R. Davie; Suzanne A.W. Fuqua

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)

Published

1997

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)