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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Autores principales:	Evelien Middeljans, Xi Wan, Pascal W Jansen, Vikram Sharma, Hendrik G Stunnenberg, Colin Logie
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f0dff07c18724e979941d68761669d59
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spelling	oai:doaj.org-article:f0dff07c18724e979941d68761669d592021-11-18T07:24:51ZSS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes.1932-620310.1371/journal.pone.0033834https://doaj.org/article/f0dff07c18724e979941d68761669d592012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22442726/?tool=EBIhttps://doaj.org/toc/1932-6203<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.Evelien MiddeljansXi WanPascal W JansenVikram SharmaHendrik G StunnenbergColin LogiePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 3, p e33834 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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.
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.
format	article
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
title	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_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_sort	ss18 together with animal-specific factors defines human baf-type swi/snf complexes.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/f0dff07c18724e979941d68761669d59
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SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexes.

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