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

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 u...

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Main Authors: Cox, P, Temperley, S, Kumar, H, Goding, C
Format: Journal article
Language:English
Published: 1988
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author Cox, P
Temperley, S
Kumar, H
Goding, C
author_facet Cox, P
Temperley, S
Kumar, H
Goding, C
author_sort Cox, P
collection OXFORD
description 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.
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spelling oxford-uuid:4076700a-c486-4f97-beb6-5e9079cf4bba2022-03-26T14:37:57ZA distinct octamer-binding protein present in malignant melanoma cells.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4076700a-c486-4f97-beb6-5e9079cf4bbaEnglishSymplectic Elements at Oxford1988Cox, PTemperley, SKumar, HGoding, CThe 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.
spellingShingle Cox, P
Temperley, S
Kumar, H
Goding, C
A distinct octamer-binding protein present in malignant melanoma cells.
title A distinct octamer-binding protein present in malignant melanoma cells.
title_full A distinct octamer-binding protein present in malignant melanoma cells.
title_fullStr A distinct octamer-binding protein present in malignant melanoma cells.
title_full_unstemmed A distinct octamer-binding protein present in malignant melanoma cells.
title_short A distinct octamer-binding protein present in malignant melanoma cells.
title_sort distinct octamer binding protein present in malignant melanoma cells
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