A distinct octamer-binding protein present in malignant melanoma cells.

Journal article

The octamer-binding proteins present in HeLa cells, B-cells and malignant melanoma cells were compared by a gel-electrophoresis DNA-binding assay. Using an extract from the malignant melanoma cells a complex was formed using a variety of octamer containing probes that was distinct from those found using either a HeLa or B-cell extract. DNAase 1 footprints and methylation interference patterns of the melanoma-specific octamer-binding protein were indistinguishable from those obtained with the HeLa factor NF-A1, except for preferential binding of the melanoma-specific factor to DNA methylated at two G residues 16 base-pairs 3' to the octamer motif. Competition analyses using a variety of wild-type and mutant probes showed that mutations affecting binding of NF-A1 similarly affected binding of the melanoma octamer-binding factor. These data also revealed the extreme flexibility of the octamer-binding site, with one probe sharing only 4 bases with the 8 base consensus sequence binding efficiently.

Authors: Cox, P; Temperley, S; Kumar, H; Goding, C

• Publication status: Published
• Journal: Nucleic acids research
• Volume: 16
• Issue: 23
• Pages: 11047-11056
• Publication date: 1988-12-01
• DOI: 10.1093/nar/16.23.11047
• EISSN: 1362-4962
• ISSN: 0305-1048
• Language: English
• Keywords: Melanoma; Base Composition; Hela Cells; B-Lymphocytes; Oligonucleotide Probes; DNA, Neoplasm; Cell Line; DNA-Binding Proteins; Deoxyribonuclease I; Humans; DNA Modification Methylases; Sequence Homology, Nucleic Acid