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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1996-1-19
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pubmed:abstractText |
The B-lymphocyte- and macrophage-specific transcription factor PU.1 is a member of the ets family of proteins. To understand how PU.1 functions as a transcription factor, we initiated a series of experiments to define its activation domain. Using deletion analysis, we showed that the activation domain of PU.1 is located in the amino-terminal half of the protein. Within this region, we identified three acidic subdomains and one glutamine-rich subdomain. The deletion of any of these subdomains resulted in a significant loss in the ability of PU.1 to transactivate in cotransfection studies. Amino acid substitution analysis showed that the activation of transcription by PU.1 requires acidic residues between amino acids 7 and 74 and a group of glutamine residues between amino acids 75 and 84. These data show that PU.1 contains two types of known activation domains and that both are required for maximal transactivation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-1323708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-1464321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-1729611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-1846049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-2142753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-2156225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-2180582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-2253872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-2673023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-2744487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-3037497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-3142690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-3943125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-6960240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-7678780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-7715708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-7799967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8007948,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8052653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8070412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8095266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8195721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8255291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8264604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8265616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8278363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8316859,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8389910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8406004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8413244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8413305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8434021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8440015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8449942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8456286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8524320-8474451
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
390-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8524320-Acids,
pubmed-meshheading:8524320-Amino Acid Sequence,
pubmed-meshheading:8524320-Binding Sites,
pubmed-meshheading:8524320-DNA-Binding Proteins,
pubmed-meshheading:8524320-Glutamine,
pubmed-meshheading:8524320-HeLa Cells,
pubmed-meshheading:8524320-Humans,
pubmed-meshheading:8524320-Molecular Sequence Data,
pubmed-meshheading:8524320-Mutagenesis, Site-Directed,
pubmed-meshheading:8524320-Peptide Mapping,
pubmed-meshheading:8524320-Retroviridae Proteins, Oncogenic,
pubmed-meshheading:8524320-Sequence Deletion,
pubmed-meshheading:8524320-Transcription Factors,
pubmed-meshheading:8524320-Transcriptional Activation,
pubmed-meshheading:8524320-Transfection
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pubmed:year |
1996
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pubmed:articleTitle |
Activation of transcription by PU.1 requires both acidic and glutamine domains.
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pubmed:affiliation |
Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis 46202, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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