Purification and characterization of a protein binding to the SP6 κ promoter : A potential role for CArG-box binding factor-A in κ transcription
(1998) In Journal of Biological Chemistry 273(30). p.18881-18890- Abstract
A protein interacting with an A-T-rich region that is a positive control element within the SP6 κ promoter was purified and identified as CArG-box binding factor-A. The purified protein was shown to interact specifically with the coding strand of single-stranded DNA and, with lower affinity, with double-stranded DNA. A mutation that inhibited binding of the protein to the A-T-rich region also aborted the transcriptional stimulatory effect of the region. Two Ets proteins, PU.1 and elf-1, that have previously been shown to bind to an adjacent DNA element were shown to physically interact with CArG- box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different splice-forms of... (More)
A protein interacting with an A-T-rich region that is a positive control element within the SP6 κ promoter was purified and identified as CArG-box binding factor-A. The purified protein was shown to interact specifically with the coding strand of single-stranded DNA and, with lower affinity, with double-stranded DNA. A mutation that inhibited binding of the protein to the A-T-rich region also aborted the transcriptional stimulatory effect of the region. Two Ets proteins, PU.1 and elf-1, that have previously been shown to bind to an adjacent DNA element were shown to physically interact with CArG- box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different splice-forms of CArG-box binding factor-A are expressed, or that the protein is subject to posttranslational modification.
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- author
- Bemark, Mats LU ; Olsson, Henric ; Heinegård, Dick LU and Leanderson, Tomas LU
- organization
- publishing date
- 1998-07-24
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 273
- issue
- 30
- pages
- 18881 - 18890
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:9668064
- scopus:0032563096
- ISSN
- 0021-9258
- DOI
- 10.1074/jbc.273.30.18881
- language
- English
- LU publication?
- yes
- id
- e68a32da-f830-4928-b33a-e1756ca00fe5
- date added to LUP
- 2023-11-28 10:21:34
- date last changed
- 2024-02-09 10:19:17
@article{e68a32da-f830-4928-b33a-e1756ca00fe5, abstract = {{<p>A protein interacting with an A-T-rich region that is a positive control element within the SP6 κ promoter was purified and identified as CArG-box binding factor-A. The purified protein was shown to interact specifically with the coding strand of single-stranded DNA and, with lower affinity, with double-stranded DNA. A mutation that inhibited binding of the protein to the A-T-rich region also aborted the transcriptional stimulatory effect of the region. Two Ets proteins, PU.1 and elf-1, that have previously been shown to bind to an adjacent DNA element were shown to physically interact with CArG- box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different splice-forms of CArG-box binding factor-A are expressed, or that the protein is subject to posttranslational modification.</p>}}, author = {{Bemark, Mats and Olsson, Henric and Heinegård, Dick and Leanderson, Tomas}}, issn = {{0021-9258}}, language = {{eng}}, month = {{07}}, number = {{30}}, pages = {{18881--18890}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Purification and characterization of a protein binding to the SP6 κ promoter : A potential role for CArG-box binding factor-A in κ transcription}}, url = {{http://dx.doi.org/10.1074/jbc.273.30.18881}}, doi = {{10.1074/jbc.273.30.18881}}, volume = {{273}}, year = {{1998}}, }