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CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality
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| Veröffentlicht in: | Nucleic acids research extent:21; volume:45; pages:10534-10554; 45(2017), 18, Seite 10534-10554; year:2017; number:18 |
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| Titel: | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality/ Helen Hoffmeister, Andreas Fuchs, Fabian Erdel, Sophia Pinz, Regina Gröbner-Ferreira, Astrid Bruckmann, Rainer Deutzmann, Uwe Schwartz, Rodrigo Maldonado, Claudia Huber, Anne-Sarah Dendorfer, Karsten Rippe, Gernot Längst |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
28 August 2017
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| Gesamtaufnahme: |
: Nucleic acids research, 45(2017), 18, Seite 10534-10554
, volume:45 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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| 520 | |a Abstract: CHD3 and CHD4 (Chromodomain Helicase DNA binding protein), two highly similar representatives of the Mi-2 subfamily of SF2 helicases, are coexpressed in many cell lines and tissues and have been reported to act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). Besides CHD proteins, NuRD contains several repressors like HDAC1/2, MTA2/3 and MBD2/3, arguing for a role as a transcriptional repressor. However, the subunit composition varies among cell- and tissue types and physiological conditions. In particular, it is unclear if CHD3 and CHD4 coexist in the same NuRD complex or whether they form distinct NuRD complexes with specific functions. We mapped the CHD composition of NuRD complexes in mammalian cells and discovered that they are isoform-specific, containing either the monomeric CHD3 or CHD4 ATPase. Both types of complexes exhibit similar intranuclear mobility, interact with HP1 and rapidly accumulate at UV-induced DNA repair sites. But, CHD3 and CHD4 exhibit distinct nuclear localization patterns in unperturbed cells, revealing a subset of specific target genes. Furthermore, CHD3 and CHD4 differ in their nucleosome remodeling and positioning behaviour in vitro. The proteins form distinct CHD3- and CHD4-NuRD complexes that do not only repress, but can just as well activate gene transcription of overlapping and specific target genes. | ||
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| author | Hoffmeister, Helen Andrea, Erdel, Fabian, Rippe, Karsten |
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| contents | Abstract: CHD3 and CHD4 (Chromodomain Helicase DNA binding protein), two highly similar representatives of the Mi-2 subfamily of SF2 helicases, are coexpressed in many cell lines and tissues and have been reported to act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). Besides CHD proteins, NuRD contains several repressors like HDAC1/2, MTA2/3 and MBD2/3, arguing for a role as a transcriptional repressor. However, the subunit composition varies among cell- and tissue types and physiological conditions. In particular, it is unclear if CHD3 and CHD4 coexist in the same NuRD complex or whether they form distinct NuRD complexes with specific functions. We mapped the CHD composition of NuRD complexes in mammalian cells and discovered that they are isoform-specific, containing either the monomeric CHD3 or CHD4 ATPase. Both types of complexes exhibit similar intranuclear mobility, interact with HP1 and rapidly accumulate at UV-induced DNA repair sites. But, CHD3 and CHD4 exhibit distinct nuclear localization patterns in unperturbed cells, revealing a subset of specific target genes. Furthermore, CHD3 and CHD4 differ in their nucleosome remodeling and positioning behaviour in vitro. The proteins form distinct CHD3- and CHD4-NuRD complexes that do not only repress, but can just as well activate gene transcription of overlapping and specific target genes. |
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| spelling | Hoffmeister, Helen Andrea 1979- (DE-588)136797334 (DE-627)587255293 (DE-576)301280576 aut, CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality Helen Hoffmeister, Andreas Fuchs, Fabian Erdel, Sophia Pinz, Regina Gröbner-Ferreira, Astrid Bruckmann, Rainer Deutzmann, Uwe Schwartz, Rodrigo Maldonado, Claudia Huber, Anne-Sarah Dendorfer, Karsten Rippe, Gernot Längst, 28 August 2017, 21, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 09.08.2018, Abstract: CHD3 and CHD4 (Chromodomain Helicase DNA binding protein), two highly similar representatives of the Mi-2 subfamily of SF2 helicases, are coexpressed in many cell lines and tissues and have been reported to act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). Besides CHD proteins, NuRD contains several repressors like HDAC1/2, MTA2/3 and MBD2/3, arguing for a role as a transcriptional repressor. However, the subunit composition varies among cell- and tissue types and physiological conditions. In particular, it is unclear if CHD3 and CHD4 coexist in the same NuRD complex or whether they form distinct NuRD complexes with specific functions. We mapped the CHD composition of NuRD complexes in mammalian cells and discovered that they are isoform-specific, containing either the monomeric CHD3 or CHD4 ATPase. Both types of complexes exhibit similar intranuclear mobility, interact with HP1 and rapidly accumulate at UV-induced DNA repair sites. But, CHD3 and CHD4 exhibit distinct nuclear localization patterns in unperturbed cells, revealing a subset of specific target genes. Furthermore, CHD3 and CHD4 differ in their nucleosome remodeling and positioning behaviour in vitro. The proteins form distinct CHD3- and CHD4-NuRD complexes that do not only repress, but can just as well activate gene transcription of overlapping and specific target genes., Erdel, Fabian VerfasserIn (DE-588)102853230X (DE-627)730877280 (DE-576)310654068 aut, Rippe, Karsten VerfasserIn (DE-588)102853261X (DE-627)730885070 (DE-576)168897989 aut, Enthalten in Nucleic acids research Oxford : Oxford Univ. Press, 1974 45(2017), 18, Seite 10534-10554 Online-Ressource (DE-627)26813250X (DE-600)1472175-2 (DE-576)07760878X 1362-4962 nnns, volume:45 year:2017 number:18 pages:10534-10554 extent:21, http://dx.doi.org/10.1093/nar/gkx711 Verlag Resolving-System kostenfrei Volltext, https://academic.oup.com/nar/article/45/18/10534/4096347 Verlag kostenfrei Volltext, http://dx.doi.org/10.1093/nar/gkx711 LFER, LFER epn:3020671663 2018-08-13T00:00:00Z |
| spellingShingle | Hoffmeister, Helen Andrea, Erdel, Fabian, Rippe, Karsten, CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality, Abstract: CHD3 and CHD4 (Chromodomain Helicase DNA binding protein), two highly similar representatives of the Mi-2 subfamily of SF2 helicases, are coexpressed in many cell lines and tissues and have been reported to act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). Besides CHD proteins, NuRD contains several repressors like HDAC1/2, MTA2/3 and MBD2/3, arguing for a role as a transcriptional repressor. However, the subunit composition varies among cell- and tissue types and physiological conditions. In particular, it is unclear if CHD3 and CHD4 coexist in the same NuRD complex or whether they form distinct NuRD complexes with specific functions. We mapped the CHD composition of NuRD complexes in mammalian cells and discovered that they are isoform-specific, containing either the monomeric CHD3 or CHD4 ATPase. Both types of complexes exhibit similar intranuclear mobility, interact with HP1 and rapidly accumulate at UV-induced DNA repair sites. But, CHD3 and CHD4 exhibit distinct nuclear localization patterns in unperturbed cells, revealing a subset of specific target genes. Furthermore, CHD3 and CHD4 differ in their nucleosome remodeling and positioning behaviour in vitro. The proteins form distinct CHD3- and CHD4-NuRD complexes that do not only repress, but can just as well activate gene transcription of overlapping and specific target genes. |
| swb_id_str | 508415691 |
| title | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality |
| title_auth | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality |
| title_full | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality Helen Hoffmeister, Andreas Fuchs, Fabian Erdel, Sophia Pinz, Regina Gröbner-Ferreira, Astrid Bruckmann, Rainer Deutzmann, Uwe Schwartz, Rodrigo Maldonado, Claudia Huber, Anne-Sarah Dendorfer, Karsten Rippe, Gernot Längst |
| title_fullStr | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality Helen Hoffmeister, Andreas Fuchs, Fabian Erdel, Sophia Pinz, Regina Gröbner-Ferreira, Astrid Bruckmann, Rainer Deutzmann, Uwe Schwartz, Rodrigo Maldonado, Claudia Huber, Anne-Sarah Dendorfer, Karsten Rippe, Gernot Längst |
| title_full_unstemmed | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality Helen Hoffmeister, Andreas Fuchs, Fabian Erdel, Sophia Pinz, Regina Gröbner-Ferreira, Astrid Bruckmann, Rainer Deutzmann, Uwe Schwartz, Rodrigo Maldonado, Claudia Huber, Anne-Sarah Dendorfer, Karsten Rippe, Gernot Längst |
| title_in_hierarchy | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality / Helen Hoffmeister, Andreas Fuchs, Fabian Erdel, Sophia Pinz, Regina Gröbner-Ferreira, Astrid Bruckmann, Rainer Deutzmann, Uwe Schwartz, Rodrigo Maldonado, Claudia Huber, Anne-Sarah Dendorfer, Karsten Rippe, Gernot Längst, |
| title_short | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality |
| title_sort | chd3 and chd4 form distinct nurd complexes with different yet overlapping functionality |
| title_unstemmed | CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality |
| url | http://dx.doi.org/10.1093/nar/gkx711, https://academic.oup.com/nar/article/45/18/10534/4096347 |
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