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...
Main Authors: | , , , |
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Format: | Journal article |
Language: | English |
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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. |
first_indexed | 2024-03-06T21:18:00Z |
format | Journal article |
id | oxford-uuid:4076700a-c486-4f97-beb6-5e9079cf4bba |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T21:18:00Z |
publishDate | 1988 |
record_format | dspace |
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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