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Nucleic Acids Research, 1988, Vol. 16, No. 23 11047-11056
© 1988

MOLECULAR BIOLOGY

A distinct octamer-binding protein present in malignant melanoma cells

P.M. Cox, S.M. Temperley*, H. Kumar{boxplus} and C.R. Godling

Marie Curie Research Institute The Chart, Oxted, Surrey RH8 OTL, UK

Department of Biochemistry and Microbiology, Irvine Building, St Andrews University, North Street, St Andrews

Roche Products Ltd, Broadwater Road, Wellwyn Garden City, Herts, UK

Received September 22, 1988. Revised November 1, 1988. Accepted November 1, 1988.

The octamer-blndlng 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-blndlng protein were indistinguishable from those obtained with the HeLa factor NF-A1, except for preferential blndlng 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.


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