Abstract:
:HeLa cell OTF-1 has been purified on the basis of its DNA binding activity and used to raise a polyclonal rabbit antiserum. This antiserum is shown to recognize both native and denatured OTF-1 from both human and a similar protein from Xenopus culture cells, but to react either more weakly or not at all with the lymphoid cell-specific OTF-2. Separately, NFIII has been purified on the basis of its ability to stimulate Adenovirus DNA replication in vitro. On denaturing polyacrylamide gels OTF-1 and NFIII exhibit identical mobility. Anti-OTF-1 antiserum recognizes NFIII and neutralizes its stimulatory effect on DNA replication. Moreover, OTF-1 can functionally replace NFIII. Taken together with previously published DNA binding data, this indicates that OTF-1 and NFIII are either very closely related or identical.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Pruijn JM,van der Vliet PC,Dathan NA,Mattaj IWdoi
10.1093/nar/17.5.1845subject
Has Abstractpub_date
1989-03-11 00:00:00pages
1845-63issue
5eissn
0305-1048issn
1362-4962journal_volume
17pub_type
杂志文章abstract::The p53 protein is crucial for adapting programs of gene expression in response to stress. Recently, we revealed that this occurs partly through the formation of stress-specific p53 binding patterns. However, the mechanisms that generate these binding patterns remain largely unknown. It is not established whether the ...
journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
pub_type: 杂志文章
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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更新日期:2008-01-01 00:00:00
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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