Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2005-3-22
pubmed:abstractText
SWI/SNF- and ISWI-based complexes have distinct yet overlapping chromatin-remodeling activities in vitro and perform different roles in vivo. This leads to the hypothesis that the distinct remodeling functions of these complexes are specifically required for distinct biological tasks. By creating and characterizing chimeric proteins of BRG1 and SNF2h, the motor proteins of human SWI/SNF- and ISWI-based complexes, respectively, we found that a region that includes the ATPase domain specifies the outcome of the remodeling reaction in vitro. A chimeric protein based on BRG1 but containing the SNF2h ATPase domain formed an intact SWI/SNF complex that remodeled like SNF2h. This altered-function complex was active for remodeling and could stimulate expression from some, but not all, SWI/SNF responsive promoters in vivo. Thus, we were able to separate domains of BRG1 responsible for function from those responsible for SWI/SNF complex formation and demonstrate that remodeling functions are not interchangeable in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glucocorticoid, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SMARCA4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SMARCA5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
805-15
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15780937-Adenosine Triphosphatases, pubmed-meshheading:15780937-Adrenal Gland Neoplasms, pubmed-meshheading:15780937-Chromatin, pubmed-meshheading:15780937-Chromatin Assembly and Disassembly, pubmed-meshheading:15780937-Chromosomal Proteins, Non-Histone, pubmed-meshheading:15780937-DNA Helicases, pubmed-meshheading:15780937-Humans, pubmed-meshheading:15780937-Nuclear Proteins, pubmed-meshheading:15780937-Nucleosomes, pubmed-meshheading:15780937-Promoter Regions, Genetic, pubmed-meshheading:15780937-Protein Structure, Tertiary, pubmed-meshheading:15780937-Receptors, Glucocorticoid, pubmed-meshheading:15780937-Recombinant Fusion Proteins, pubmed-meshheading:15780937-Transcription, Genetic, pubmed-meshheading:15780937-Transcription Factors, pubmed-meshheading:15780937-Transcriptional Activation, pubmed-meshheading:15780937-Tumor Cells, Cultured, pubmed-meshheading:15780937-Zinc Fingers
pubmed:year
2005
pubmed:articleTitle
Swapping function of two chromatin remodeling complexes.
pubmed:affiliation
Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.