Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2002-2-11
pubmed:databankReference
pubmed:abstractText
A global transcriptional co-activator, the SNF/SWI complex, has been characterized as a chromatin remodeling factor that enhances accessibility of the transcriptional machinery to DNA within a repressive chromatin structure. On the other hand, mutations in some human SNF/SWI complex components have been linked to tumor formation. We show here that SYT, a partner protein generating the synovial sarcoma fusion protein SYT-SSX, associates with native human SNF/SWI complexes. The SYT protein has a unique QPGY domain, which is also present in the largest subunits, p250 and the newly identified homolog p250R, of the corresponding SNF/SWI complexes. The C-terminal region (amino acids 310-387) of SSX1, comprising the SSX1 portion of the SYT-SSX1 fusion protein, binds strongly to core histones and oligonucleosomes in vitro and directs nuclear localization of a green fluorescence protein fusion protein. Experiments with serial C-terminal deletion mutants of SSX1 indicate that these properties map to a common region and also correlate with the previously demonstrated anchorage-independent colony formation activity of SYT-SSX in Rat 3Y1 cells. These data suggest that SYT-SSX interferes with the function of either the SNF/SWI complexes or another SYT-interacting co-activator, p300, by changing their targeted localization or by directly inhibiting their chromatin remodeling activities.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5498-505
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11734557-Amino Acid Sequence, pubmed-meshheading:11734557-Cell Line, pubmed-meshheading:11734557-Cell Nucleus, pubmed-meshheading:11734557-Chromatin, pubmed-meshheading:11734557-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11734557-Gene Deletion, pubmed-meshheading:11734557-Glutathione Transferase, pubmed-meshheading:11734557-HeLa Cells, pubmed-meshheading:11734557-Histones, pubmed-meshheading:11734557-Humans, pubmed-meshheading:11734557-Immunoblotting, pubmed-meshheading:11734557-Models, Genetic, pubmed-meshheading:11734557-Molecular Sequence Data, pubmed-meshheading:11734557-Mutagenesis, Site-Directed, pubmed-meshheading:11734557-Plasmids, pubmed-meshheading:11734557-Protein Binding, pubmed-meshheading:11734557-Protein Structure, Tertiary, pubmed-meshheading:11734557-Protein-Serine-Threonine Kinases, pubmed-meshheading:11734557-Proteins, pubmed-meshheading:11734557-Proto-Oncogene Proteins, pubmed-meshheading:11734557-Recombinant Fusion Proteins, pubmed-meshheading:11734557-Repressor Proteins, pubmed-meshheading:11734557-Transcription, Genetic, pubmed-meshheading:11734557-Transcription Factors
pubmed:year
2002
pubmed:articleTitle
SYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histones.
pubmed:affiliation
Laboratory of Biochemistry and Molecular Biology and Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10021, USA. hykato@nih.go.jp
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.