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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
1992-10-7
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pubmed:abstractText |
The human ETS1 proto-oncogene proteins have been isolated from the T-cell leukemia line, CEM, by immunoaffinity chromatography and their identity confirmed by NH2-terminal amino acid sequencing. Incubation of CEM cells with N alpha-p-tosyl-L-lysine chloromethyl ketone (TLCK) indicates that ETS proteins can be modified in their cellular context and that pretreatment of the cells with N-ethylmaleimide (NEM) protects ETS1 proteins from TLCK modification. These data show that ETS1 proteins can exist in at least two different states, -SH-available and -SH-protected. Renatured human ETS1 has DNA sequence-specific binding to the PEA3 (CAGGAAGT) motif. The ETS1.PEA3 complex can be observed by electrophoretic mobility shift assays (EMSA). Purified ETS1 retards a band which is exactly the same size as a complex that is retarded from nuclear extracts prepared from CEM cells. Reduced ETS1 is required to form the ETS1.PEA3 complex, however; modification of the ETS1 -SH groups by either NEM or by TLCk does not inhibit formation of the complex. The ETS1.PEA3 complex formed with TLCK-modified ETS1 has a slower mobility than the complex formed with unmodified ETS1. Zone sedimentation analysis of purified ETS1 indicates that it is the monomer of ETS1 which binds to the PEA3 oligonucleotide.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ETS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Protein c-ets-1,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-ets,
http://linkedlifedata.com/resource/pubmed/chemical/Tosyllysine Chloromethyl Ketone,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17957-65
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1517230-Amino Acid Sequence,
pubmed-meshheading:1517230-Antibodies, Monoclonal,
pubmed-meshheading:1517230-Base Sequence,
pubmed-meshheading:1517230-Cell Line,
pubmed-meshheading:1517230-Cell Nucleus,
pubmed-meshheading:1517230-Centrifugation, Zonal,
pubmed-meshheading:1517230-Chromatography, Affinity,
pubmed-meshheading:1517230-DNA-Binding Proteins,
pubmed-meshheading:1517230-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1517230-Ethylmaleimide,
pubmed-meshheading:1517230-Humans,
pubmed-meshheading:1517230-Leukemia, T-Cell,
pubmed-meshheading:1517230-Molecular Sequence Data,
pubmed-meshheading:1517230-Oligodeoxyribonucleotides,
pubmed-meshheading:1517230-Oligopeptides,
pubmed-meshheading:1517230-Proto-Oncogene Protein c-ets-1,
pubmed-meshheading:1517230-Proto-Oncogene Proteins,
pubmed-meshheading:1517230-Proto-Oncogene Proteins c-ets,
pubmed-meshheading:1517230-Tosyllysine Chloromethyl Ketone,
pubmed-meshheading:1517230-Transcription Factors
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pubmed:year |
1992
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pubmed:articleTitle |
Human ETS1 oncoprotein. Purification, isoforms, -SH modification, and DNA sequence-specific binding.
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pubmed:affiliation |
Laboratory of Cellular Biochemistry, Program Resources, Inc./DynCorp, Frederick Cancer Research and Development Center, Maryland.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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