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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1990-7-18
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pubmed:abstractText |
Pit-1 is a member of a family of transcription factors sharing two regions of homology: a highly conserved POU-specific (POUS) domain and a more divergent homeodomain (POUHD). Analysis of mutant Pit-1 proteins suggests that, while the POUHD is required and sufficient for low affinity DNA binding, the POUS domain is necessary for high affinity binding and accurate recognition of natural Pit-1 response elements. Pit-1 is monomeric in solution but associates as a dimer on its DNA response element, exhibiting DNA-dependent protein-protein interactions requiring the POUS domain. Analysis of alpha-helical domains and conserved structures in Pit-1 suggests that POU domain proteins interact with their DNA recognition sites differently than classic homeodomain proteins, with both the POUHD and the POUS domain contacting DNA. Transcriptional activity of Pit-1 on enhancer elements is conferred primarily by a Ser- and Thr-rich N-terminal region unrelated to other known transcription-activating motifs.
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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 |
Jun
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pubmed:issn |
0092-8674
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1021-33
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2350782-Algorithms,
pubmed-meshheading:2350782-Animals,
pubmed-meshheading:2350782-Base Sequence,
pubmed-meshheading:2350782-Binding Sites,
pubmed-meshheading:2350782-DNA,
pubmed-meshheading:2350782-DNA-Binding Proteins,
pubmed-meshheading:2350782-Kinetics,
pubmed-meshheading:2350782-Molecular Sequence Data,
pubmed-meshheading:2350782-Mutation,
pubmed-meshheading:2350782-Oligodeoxyribonucleotides,
pubmed-meshheading:2350782-Oligonucleotide Probes,
pubmed-meshheading:2350782-Plasmids,
pubmed-meshheading:2350782-Polymerase Chain Reaction,
pubmed-meshheading:2350782-Protein Binding,
pubmed-meshheading:2350782-Protein Conformation,
pubmed-meshheading:2350782-Restriction Mapping,
pubmed-meshheading:2350782-Transcription Factor Pit-1,
pubmed-meshheading:2350782-Transcription Factors,
pubmed-meshheading:2350782-Transcriptional Activation,
pubmed-meshheading:2350782-Transfection
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pubmed:year |
1990
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pubmed:articleTitle |
The POU-specific domain of Pit-1 is essential for sequence-specific, high affinity DNA binding and DNA-dependent Pit-1-Pit-1 interactions.
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pubmed:affiliation |
Howard Hughes Medical Institute, School of Medicine, University of California, San Diego, La Jolla 92093.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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