Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates

Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. Howev...
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Autor*in:	Dryhurst, Deanna [verfasserIn] Ishibashi, Toyotaka Rose, Kristie L Eirín-López, José M McDonald, Darin Silva-Moreno, Begonia Veldhoen, Nik Helbing, Caren C Hendzel, Michael J Shabanowitz, Jeffrey Hunt, Donald F Ausió, Juan

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2009

Schlagwörter:	HeLa Cell Sodium Butyrate Nocodazole Histone Variant Proximal Promoter Region

Anmerkung:	© Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (

Übergeordnetes Werk:	Enthalten in: BMC biology - Berlin : Springer, 2003, 7(2009), 1 vom: 14. Dez.
Übergeordnetes Werk:	volume:7 ; year:2009 ; number:1 ; day:14 ; month:12

Links:	Volltext

DOI / URN:	10.1186/1741-7007-7-86

Katalog-ID:	SPR028327853

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520			\|a Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence.
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Indexfelder

author_variant	d d dd t i ti k l r kl klr j m e l jme jmel d m dm b s m bsm n v nv c c h cc cch m j h mj mjh j s js d f h df dfh j a ja
matchkey_str	article:17417007:2009----::hrceiainfhhsoe2zad2zio
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publishDate	2009
allfields	10.1186/1741-7007-7-86 doi (DE-627)SPR028327853 (SPR)1741-7007-7-86-e DE-627 ger DE-627 rakwb eng Dryhurst, Deanna verfasserin aut Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. HeLa Cell (dpeaa)DE-He213 Sodium Butyrate (dpeaa)DE-He213 Nocodazole (dpeaa)DE-He213 Histone Variant (dpeaa)DE-He213 Proximal Promoter Region (dpeaa)DE-He213 Ishibashi, Toyotaka aut Rose, Kristie L aut Eirín-López, José M aut McDonald, Darin aut Silva-Moreno, Begonia aut Veldhoen, Nik aut Helbing, Caren C aut Hendzel, Michael J aut Shabanowitz, Jeffrey aut Hunt, Donald F aut Ausió, Juan aut Enthalten in BMC biology Berlin : Springer, 2003 7(2009), 1 vom: 14. Dez. (DE-627)377757241 (DE-600)2133020-7 1741-7007 nnns volume:7 year:2009 number:1 day:14 month:12 https://dx.doi.org/10.1186/1741-7007-7-86 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2009 1 14 12
spelling	10.1186/1741-7007-7-86 doi (DE-627)SPR028327853 (SPR)1741-7007-7-86-e DE-627 ger DE-627 rakwb eng Dryhurst, Deanna verfasserin aut Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. HeLa Cell (dpeaa)DE-He213 Sodium Butyrate (dpeaa)DE-He213 Nocodazole (dpeaa)DE-He213 Histone Variant (dpeaa)DE-He213 Proximal Promoter Region (dpeaa)DE-He213 Ishibashi, Toyotaka aut Rose, Kristie L aut Eirín-López, José M aut McDonald, Darin aut Silva-Moreno, Begonia aut Veldhoen, Nik aut Helbing, Caren C aut Hendzel, Michael J aut Shabanowitz, Jeffrey aut Hunt, Donald F aut Ausió, Juan aut Enthalten in BMC biology Berlin : Springer, 2003 7(2009), 1 vom: 14. Dez. (DE-627)377757241 (DE-600)2133020-7 1741-7007 nnns volume:7 year:2009 number:1 day:14 month:12 https://dx.doi.org/10.1186/1741-7007-7-86 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2009 1 14 12
allfields_unstemmed	10.1186/1741-7007-7-86 doi (DE-627)SPR028327853 (SPR)1741-7007-7-86-e DE-627 ger DE-627 rakwb eng Dryhurst, Deanna verfasserin aut Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. HeLa Cell (dpeaa)DE-He213 Sodium Butyrate (dpeaa)DE-He213 Nocodazole (dpeaa)DE-He213 Histone Variant (dpeaa)DE-He213 Proximal Promoter Region (dpeaa)DE-He213 Ishibashi, Toyotaka aut Rose, Kristie L aut Eirín-López, José M aut McDonald, Darin aut Silva-Moreno, Begonia aut Veldhoen, Nik aut Helbing, Caren C aut Hendzel, Michael J aut Shabanowitz, Jeffrey aut Hunt, Donald F aut Ausió, Juan aut Enthalten in BMC biology Berlin : Springer, 2003 7(2009), 1 vom: 14. Dez. (DE-627)377757241 (DE-600)2133020-7 1741-7007 nnns volume:7 year:2009 number:1 day:14 month:12 https://dx.doi.org/10.1186/1741-7007-7-86 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2009 1 14 12
allfieldsGer	10.1186/1741-7007-7-86 doi (DE-627)SPR028327853 (SPR)1741-7007-7-86-e DE-627 ger DE-627 rakwb eng Dryhurst, Deanna verfasserin aut Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. HeLa Cell (dpeaa)DE-He213 Sodium Butyrate (dpeaa)DE-He213 Nocodazole (dpeaa)DE-He213 Histone Variant (dpeaa)DE-He213 Proximal Promoter Region (dpeaa)DE-He213 Ishibashi, Toyotaka aut Rose, Kristie L aut Eirín-López, José M aut McDonald, Darin aut Silva-Moreno, Begonia aut Veldhoen, Nik aut Helbing, Caren C aut Hendzel, Michael J aut Shabanowitz, Jeffrey aut Hunt, Donald F aut Ausió, Juan aut Enthalten in BMC biology Berlin : Springer, 2003 7(2009), 1 vom: 14. Dez. (DE-627)377757241 (DE-600)2133020-7 1741-7007 nnns volume:7 year:2009 number:1 day:14 month:12 https://dx.doi.org/10.1186/1741-7007-7-86 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2009 1 14 12
allfieldsSound	10.1186/1741-7007-7-86 doi (DE-627)SPR028327853 (SPR)1741-7007-7-86-e DE-627 ger DE-627 rakwb eng Dryhurst, Deanna verfasserin aut Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. HeLa Cell (dpeaa)DE-He213 Sodium Butyrate (dpeaa)DE-He213 Nocodazole (dpeaa)DE-He213 Histone Variant (dpeaa)DE-He213 Proximal Promoter Region (dpeaa)DE-He213 Ishibashi, Toyotaka aut Rose, Kristie L aut Eirín-López, José M aut McDonald, Darin aut Silva-Moreno, Begonia aut Veldhoen, Nik aut Helbing, Caren C aut Hendzel, Michael J aut Shabanowitz, Jeffrey aut Hunt, Donald F aut Ausió, Juan aut Enthalten in BMC biology Berlin : Springer, 2003 7(2009), 1 vom: 14. Dez. (DE-627)377757241 (DE-600)2133020-7 1741-7007 nnns volume:7 year:2009 number:1 day:14 month:12 https://dx.doi.org/10.1186/1741-7007-7-86 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2009 1 14 12
language	English
source	Enthalten in BMC biology 7(2009), 1 vom: 14. Dez. volume:7 year:2009 number:1 day:14 month:12
sourceStr	Enthalten in BMC biology 7(2009), 1 vom: 14. Dez. volume:7 year:2009 number:1 day:14 month:12
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	HeLa Cell Sodium Butyrate Nocodazole Histone Variant Proximal Promoter Region
isfreeaccess_bool	false
container_title	BMC biology
authorswithroles_txt_mv	Dryhurst, Deanna @@aut@@ Ishibashi, Toyotaka @@aut@@ Rose, Kristie L @@aut@@ Eirín-López, José M @@aut@@ McDonald, Darin @@aut@@ Silva-Moreno, Begonia @@aut@@ Veldhoen, Nik @@aut@@ Helbing, Caren C @@aut@@ Hendzel, Michael J @@aut@@ Shabanowitz, Jeffrey @@aut@@ Hunt, Donald F @@aut@@ Ausió, Juan @@aut@@
publishDateDaySort_date	2009-12-14T00:00:00Z
hierarchy_top_id	377757241
id	SPR028327853
language_de	englisch
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author	Dryhurst, Deanna
spellingShingle	Dryhurst, Deanna misc HeLa Cell misc Sodium Butyrate misc Nocodazole misc Histone Variant misc Proximal Promoter Region Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
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topic_title	Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates HeLa Cell (dpeaa)DE-He213 Sodium Butyrate (dpeaa)DE-He213 Nocodazole (dpeaa)DE-He213 Histone Variant (dpeaa)DE-He213 Proximal Promoter Region (dpeaa)DE-He213
topic	misc HeLa Cell misc Sodium Butyrate misc Nocodazole misc Histone Variant misc Proximal Promoter Region
topic_unstemmed	misc HeLa Cell misc Sodium Butyrate misc Nocodazole misc Histone Variant misc Proximal Promoter Region
topic_browse	misc HeLa Cell misc Sodium Butyrate misc Nocodazole misc Histone Variant misc Proximal Promoter Region
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
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title	Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
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title_full	Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
author_sort	Dryhurst, Deanna
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author_browse	Dryhurst, Deanna Ishibashi, Toyotaka Rose, Kristie L Eirín-López, José M McDonald, Darin Silva-Moreno, Begonia Veldhoen, Nik Helbing, Caren C Hendzel, Michael J Shabanowitz, Jeffrey Hunt, Donald F Ausió, Juan
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format_se	Elektronische Aufsätze
author-letter	Dryhurst, Deanna
doi_str_mv	10.1186/1741-7007-7-86
title_sort	characterization of the histone h2a.z-1 and h2a.z-2 isoforms in vertebrates
title_auth	Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
abstract	Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstractGer	Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstract_unstemmed	Background Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence. © Dryhurst et al; licensee BioMed Central Ltd. 2009. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
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title_short	Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
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author2	Ishibashi, Toyotaka Rose, Kristie L Eirín-López, José M McDonald, Darin Silva-Moreno, Begonia Veldhoen, Nik Helbing, Caren C Hendzel, Michael J Shabanowitz, Jeffrey Hunt, Donald F Ausió, Juan
author2Str	Ishibashi, Toyotaka Rose, Kristie L Eirín-López, José M McDonald, Darin Silva-Moreno, Begonia Veldhoen, Nik Helbing, Caren C Hendzel, Michael J Shabanowitz, Jeffrey Hunt, Donald F Ausió, Juan
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Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates

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