rdf:type |
|
lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0292369,
umls-concept:C0449432,
umls-concept:C0812273,
umls-concept:C0919528,
umls-concept:C1167093,
umls-concept:C1179435,
umls-concept:C1335857,
umls-concept:C1519134,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248,
umls-concept:C1707271
|
pubmed:issue |
8
|
pubmed:dateCreated |
1998-5-13
|
pubmed:abstractText |
The ALL-1 gene was discovered by virtue of its involvement in human acute leukemia. Its Drosophila homolog trithorax (trx) is a member of the trx-Polycomb gene family, which maintains correct spatial expression of the Antennapedia and bithorax complexes during embryogenesis. The C-terminal SET domain of ALL-1 and TRITHORAX (TRX) is a 150-aa motif, highly conserved during evolution. We performed yeast two hybrid screening of Drosophila cDNA library and detected interaction between a TRX polypeptide spanning SET and the SNR1 protein. SNR1 is a product of snr1, which is classified as a trx group gene. We found parallel interaction in yeast between the SET domain of ALL-1 and the human homolog of SNR1, INI1 (hSNF5). These results were confirmed by in vitro binding studies and by demonstrating coimmunoprecipitation of the proteins from cultured cells and/or transgenic flies. Epitope-tagged SNR1 was detected at discrete sites on larval salivary gland polytene chromosomes, and these sites colocalized with around one-half of TRX binding sites. Because SNR1 and INI1 are constituents of the SWI/SNF complex, which acts to remodel chromatin and consequently to activate transcription, the interactions we observed suggest a mechanism by which the SWI/SNF complex is recruited to ALL-1/trx targets through physical interactions between the C-terminal domains of ALL-1 and TRX and INI1/SNR1.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-103000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-1353445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-1423624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-1423625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-1898775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-2107543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7579694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7662368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7739891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7744011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7801128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7837391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7915232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7935842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-7958911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8096812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8101171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8127913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8159677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8248257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8413234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8467801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8521501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8608939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8722173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8725238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8825476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-8895581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-9020364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-9247308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-9326598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9539705-9398665
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MLL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Myeloid-Lymphoid Leukemia Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Snr1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Trl protein, Drosophila
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
14
|
pubmed:volume |
95
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4152-7
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:9539705-Amino Acid Sequence,
pubmed-meshheading:9539705-Animals,
pubmed-meshheading:9539705-Animals, Genetically Modified,
pubmed-meshheading:9539705-Biological Evolution,
pubmed-meshheading:9539705-Cell Line,
pubmed-meshheading:9539705-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9539705-Cloning, Molecular,
pubmed-meshheading:9539705-Conserved Sequence,
pubmed-meshheading:9539705-DNA-Binding Proteins,
pubmed-meshheading:9539705-Drosophila Proteins,
pubmed-meshheading:9539705-Humans,
pubmed-meshheading:9539705-Leukemia,
pubmed-meshheading:9539705-Myeloid-Lymphoid Leukemia Protein,
pubmed-meshheading:9539705-Proto-Oncogenes,
pubmed-meshheading:9539705-Recombinant Proteins,
pubmed-meshheading:9539705-Transcription Factors,
pubmed-meshheading:9539705-Transfection,
pubmed-meshheading:9539705-Tumor Cells, Cultured,
pubmed-meshheading:9539705-Zinc Fingers
|
pubmed:year |
1998
|
pubmed:articleTitle |
The C-terminal SET domains of ALL-1 and TRITHORAX interact with the INI1 and SNR1 proteins, components of the SWI/SNF complex.
|
pubmed:affiliation |
Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|