SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes.
<h4>Background</h4>Nucleosome translocation along DNA is catalyzed by eukaryotic SNF2-type ATPases. One class of SNF2-ATPases is distinguished by the presence of a C-terminal bromodomain and is conserved from yeast to man and plants. This class of SNF2 enzymes forms rather large protein...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22442726/?tool=EBI |
| _version_ | 1818845945575505920 |
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| author | Evelien Middeljans Xi Wan Pascal W Jansen Vikram Sharma Hendrik G Stunnenberg Colin Logie |
| author_facet | Evelien Middeljans Xi Wan Pascal W Jansen Vikram Sharma Hendrik G Stunnenberg Colin Logie |
| author_sort | Evelien Middeljans |
| collection | DOAJ |
| description | <h4>Background</h4>Nucleosome translocation along DNA is catalyzed by eukaryotic SNF2-type ATPases. One class of SNF2-ATPases is distinguished by the presence of a C-terminal bromodomain and is conserved from yeast to man and plants. This class of SNF2 enzymes forms rather large protein complexes that are collectively called SWI/SNF complexes. They are involved in transcription and DNA repair. Two broad types of SWI/SNF complexes have been reported in the literature; PBAF and BAF. These are distinguished by the inclusion or not of polybromo and several ARID subunits. Here we investigated human SS18, a protein that is conserved in plants and animals. SS18 is a putative SWI/SNF subunit which has been implicated in the etiology of synovial sarcomas by virtue of being a target for oncogenic chromosomal translocations that underlie synovial sarcomas.<h4>Methodology/principal findings</h4>We pursued a proteomic approach whereby the SS18 open reading frame was fused to a tandem affinity purification tag and expressed in amenable human cells. The fusion permitted efficient and exclusive purification of so-called BAF-type SWI/SNF complexes which bear ARID1A/BAF250a or ARID1B/BAF250b subunits. This demonstrates that SS18 is a BAF subtype-specific SWI/SNF complex subunit. The same result was obtained when using the SS18-SSX1 oncogenic translocation product. Furthermore, SS18L1, DPF1, DPF2, DPF3, BRD9, BCL7A, BCL7B and BCL7C were identified. 'Complex walking' showed that they all co-purify with each other, defining human BAF-type complexes. By contrast,we demonstrate that human PHF10 is part of the PBAF complex, which harbors both ARID2/BAF200 and polybromo/BAF180 subunits, but not SS18 and nor the above BAF-specific subunits.<h4>Conclusions/significance</h4>SWI/SNF complexes are found in most eukaryotes and in the course of evolution new SWI/SNF subunits appeared. SS18 is found in plants as well as animals. Our results suggest that in both protostome and deuterostome animals, a class of BAF-type SWI/SNF complexes will be found that harbor SS18 or its paralogs, along with ARID1, DPF and BCL7 paralogs. Those BAF complexes are proteomically distinct from the eukaryote-wide PBAF-type SWI/SNF complexes. Finally, our results suggests that the human bromodomain factors BRD7 and BRD9 associate with PBAF and BAF, respectively. |
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| id | doaj.art-f0dff07c18724e979941d68761669d59 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-19T05:37:43Z |
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| spelling | doaj.art-f0dff07c18724e979941d68761669d592022-12-21T20:34:06ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0173e3383410.1371/journal.pone.0033834SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes.Evelien MiddeljansXi WanPascal W JansenVikram SharmaHendrik G StunnenbergColin Logie<h4>Background</h4>Nucleosome translocation along DNA is catalyzed by eukaryotic SNF2-type ATPases. One class of SNF2-ATPases is distinguished by the presence of a C-terminal bromodomain and is conserved from yeast to man and plants. This class of SNF2 enzymes forms rather large protein complexes that are collectively called SWI/SNF complexes. They are involved in transcription and DNA repair. Two broad types of SWI/SNF complexes have been reported in the literature; PBAF and BAF. These are distinguished by the inclusion or not of polybromo and several ARID subunits. Here we investigated human SS18, a protein that is conserved in plants and animals. SS18 is a putative SWI/SNF subunit which has been implicated in the etiology of synovial sarcomas by virtue of being a target for oncogenic chromosomal translocations that underlie synovial sarcomas.<h4>Methodology/principal findings</h4>We pursued a proteomic approach whereby the SS18 open reading frame was fused to a tandem affinity purification tag and expressed in amenable human cells. The fusion permitted efficient and exclusive purification of so-called BAF-type SWI/SNF complexes which bear ARID1A/BAF250a or ARID1B/BAF250b subunits. This demonstrates that SS18 is a BAF subtype-specific SWI/SNF complex subunit. The same result was obtained when using the SS18-SSX1 oncogenic translocation product. Furthermore, SS18L1, DPF1, DPF2, DPF3, BRD9, BCL7A, BCL7B and BCL7C were identified. 'Complex walking' showed that they all co-purify with each other, defining human BAF-type complexes. By contrast,we demonstrate that human PHF10 is part of the PBAF complex, which harbors both ARID2/BAF200 and polybromo/BAF180 subunits, but not SS18 and nor the above BAF-specific subunits.<h4>Conclusions/significance</h4>SWI/SNF complexes are found in most eukaryotes and in the course of evolution new SWI/SNF subunits appeared. SS18 is found in plants as well as animals. Our results suggest that in both protostome and deuterostome animals, a class of BAF-type SWI/SNF complexes will be found that harbor SS18 or its paralogs, along with ARID1, DPF and BCL7 paralogs. Those BAF complexes are proteomically distinct from the eukaryote-wide PBAF-type SWI/SNF complexes. Finally, our results suggests that the human bromodomain factors BRD7 and BRD9 associate with PBAF and BAF, respectively.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22442726/?tool=EBI |
| spellingShingle | Evelien Middeljans Xi Wan Pascal W Jansen Vikram Sharma Hendrik G Stunnenberg Colin Logie SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes. PLoS ONE |
| title | SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes. |
| title_full | SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes. |
| title_fullStr | SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes. |
| title_full_unstemmed | SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes. |
| title_short | SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes. |
| title_sort | ss18 together with animal specific factors defines human baf type swi snf complexes |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22442726/?tool=EBI |
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