Genome-wide patterns of histone modifications in yeast
Key Points The availability of antibodies that are directed against specific histone-modification sites has allowed the mapping of these sites at the whole-genome level using microarrays. Recent data in Saccharomyces cerevisiae are analysed to ask whether unique histone-modification patterns have sp...
Gespeichert in:
Veröffentlicht in: | Nature reviews. Molecular cell biology 2006-09, Vol.7 (9), p.657-666 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 666 |
---|---|
container_issue | 9 |
container_start_page | 657 |
container_title | Nature reviews. Molecular cell biology |
container_volume | 7 |
creator | Millar, Catherine B Grunstein, Michael |
description | Key Points
The availability of antibodies that are directed against specific histone-modification sites has allowed the mapping of these sites at the whole-genome level using microarrays. Recent data in
Saccharomyces cerevisiae
are analysed to ask whether unique histone-modification patterns have specific functions.
The preferences of enzymes for particular histone sites and chromosomal locations are described. Different enzymes can affect the same genomic regions to generate unique patterns of modifications.
In particular, there are differences between the histone-modification patterns of heterochromatin, subtelomeric heterochromatin-adjacent regions, centromeric chromatin, promoters and coding regions. The roles of histone-modification patterns at these domains are discussed.
The fully deacetylated, demethylated state is necessary for repression of gene activity in heterochromatin. Domains that are partially deacetylated might be activated more easily.
Both acetylation and deacetylation are important for gene activity. Certain sites, including H4K16, are hypoacetylated at active genes, and histone deacetylases that deacetylate H4K16 (for example, Hos2) have also been described as activators of transcription.
Hypoacetylation and methylation of certain lysine residues have been shown to affect the binding of chromosomal proteins to target genes. These studies also provide a link between the methylation of a lysine residue (H3K36) and the recruitment of the histone deacetylase Rpd3 to a gene.
Finally, the availability of similar studies in
Schizosaccharomyces pombe
, which is widely divergent in evolution from
S. cerevisiae
, suggests that the findings above might be extrapolated to other eukaryotes.
The recent mapping of histone modifications across the
Saccharomyces cerevisiae
genome has allowed the analysis of how combinations of modified and unmodified chromatin states relate to each other and particularly to chromosomal landmarks, such as heterochromatin, centromeres, promoters and coding regions.
Post-translational histone modifications and histone variants generate complexity in chromatin to enable the many functions of the chromosome. Recent studies have mapped histone modifications across the
Saccharomyces cerevisiae
genome. These experiments describe how combinations of modified and unmodified states relate to each other and particularly to chromosomal landmarks that include heterochromatin, subtelomeric chromatin, centromeres, origins of replicat |
doi_str_mv | 10.1038/nrm1986 |
format | Article |
fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_68768139</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A188912138</galeid><sourcerecordid>A188912138</sourcerecordid><originalsourceid>FETCH-LOGICAL-c493t-922d0e8db6c89c4830ff83da910ac0ad05853be5c5827bb93b059433d00eb8643</originalsourceid><addsrcrecordid>eNqF0VtrFDEUB_Agir0ofgJlUPDyMDWXSSZ5LEVroSB4eQ6Z5MyaspNskwzab98ss7asCpKHhJxf_nByEHpG8AnBTL4PaSJKigfokHQ9aTGW-OHduacH6CjnK4yJID1_jA6IUIT2hB8icQ4hTtD-9A6ajSkFUshNHJsfPpcYoJmi86O3pvhYCz40N2ByeYIejWad4eluP0bfP374dvapvfx8fnF2etnaTrHSKkodBukGYaWynWR4HCVzRhFsLDYOc8nZANxySfthUGzAXHWMOYxhkKJjx-j1krtJ8XqGXPTks4X12gSIc9ZC9kISpv4LKRa051hW-PIPeBXnFGoTmtJOCM6IqOjVglZmDdqHMZZk7DZRnxIp6-cRto06-Yeqy8Hkbf280df7vQfv9h5UU-BXWZk5Z33x9cu-fbNYm2LOCUa9SX4y6UYTrLcz17uZV_li19E8TODu3W7IFbxdQK6lsIJ03_LfWc8XGkyZE9xl_a7fAmrXulg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>224665316</pqid></control><display><type>article</type><title>Genome-wide patterns of histone modifications in yeast</title><source>MEDLINE</source><source>SpringerLink_现刊</source><source>Nature</source><creator>Millar, Catherine B ; Grunstein, Michael</creator><creatorcontrib>Millar, Catherine B ; Grunstein, Michael</creatorcontrib><description>Key Points
The availability of antibodies that are directed against specific histone-modification sites has allowed the mapping of these sites at the whole-genome level using microarrays. Recent data in
Saccharomyces cerevisiae
are analysed to ask whether unique histone-modification patterns have specific functions.
The preferences of enzymes for particular histone sites and chromosomal locations are described. Different enzymes can affect the same genomic regions to generate unique patterns of modifications.
In particular, there are differences between the histone-modification patterns of heterochromatin, subtelomeric heterochromatin-adjacent regions, centromeric chromatin, promoters and coding regions. The roles of histone-modification patterns at these domains are discussed.
The fully deacetylated, demethylated state is necessary for repression of gene activity in heterochromatin. Domains that are partially deacetylated might be activated more easily.
Both acetylation and deacetylation are important for gene activity. Certain sites, including H4K16, are hypoacetylated at active genes, and histone deacetylases that deacetylate H4K16 (for example, Hos2) have also been described as activators of transcription.
Hypoacetylation and methylation of certain lysine residues have been shown to affect the binding of chromosomal proteins to target genes. These studies also provide a link between the methylation of a lysine residue (H3K36) and the recruitment of the histone deacetylase Rpd3 to a gene.
Finally, the availability of similar studies in
Schizosaccharomyces pombe
, which is widely divergent in evolution from
S. cerevisiae
, suggests that the findings above might be extrapolated to other eukaryotes.
The recent mapping of histone modifications across the
Saccharomyces cerevisiae
genome has allowed the analysis of how combinations of modified and unmodified chromatin states relate to each other and particularly to chromosomal landmarks, such as heterochromatin, centromeres, promoters and coding regions.
Post-translational histone modifications and histone variants generate complexity in chromatin to enable the many functions of the chromosome. Recent studies have mapped histone modifications across the
Saccharomyces cerevisiae
genome. These experiments describe how combinations of modified and unmodified states relate to each other and particularly to chromosomal landmarks that include heterochromatin, subtelomeric chromatin, centromeres, origins of replication, promoters and coding regions. Such patterns might be important for the regulation of heterochromatin-mediated silencing, chromosome segregation, DNA replication and gene expression.</description><identifier>ISSN: 1471-0072</identifier><identifier>EISSN: 1471-0080</identifier><identifier>DOI: 10.1038/nrm1986</identifier><identifier>PMID: 16912715</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Biochemistry ; Biomedical and Life Sciences ; Cancer Research ; Cell Biology ; Cell cycle ; Chromosomes, Fungal - genetics ; Chromosomes, Fungal - metabolism ; Deoxyribonucleic acid ; Developmental Biology ; DNA ; DNA methylation ; DNA Replication - genetics ; Enzymes ; Gene Expression Regulation, Fungal - genetics ; Gene Silencing - physiology ; Genome, Fungal - genetics ; Genomes ; Heterochromatin - genetics ; Heterochromatin - metabolism ; Histones - genetics ; Histones - metabolism ; Life Sciences ; Protein Processing, Post-Translational - genetics ; Proteins ; review-article ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Stem Cells ; Yeast ; Yeasts</subject><ispartof>Nature reviews. Molecular cell biology, 2006-09, Vol.7 (9), p.657-666</ispartof><rights>Springer Nature Limited 2006</rights><rights>COPYRIGHT 2006 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Sep 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c493t-922d0e8db6c89c4830ff83da910ac0ad05853be5c5827bb93b059433d00eb8643</citedby><cites>FETCH-LOGICAL-c493t-922d0e8db6c89c4830ff83da910ac0ad05853be5c5827bb93b059433d00eb8643</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nrm1986$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nrm1986$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,2727,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16912715$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Millar, Catherine B</creatorcontrib><creatorcontrib>Grunstein, Michael</creatorcontrib><title>Genome-wide patterns of histone modifications in yeast</title><title>Nature reviews. Molecular cell biology</title><addtitle>Nat Rev Mol Cell Biol</addtitle><addtitle>Nat Rev Mol Cell Biol</addtitle><description>Key Points
The availability of antibodies that are directed against specific histone-modification sites has allowed the mapping of these sites at the whole-genome level using microarrays. Recent data in
Saccharomyces cerevisiae
are analysed to ask whether unique histone-modification patterns have specific functions.
The preferences of enzymes for particular histone sites and chromosomal locations are described. Different enzymes can affect the same genomic regions to generate unique patterns of modifications.
In particular, there are differences between the histone-modification patterns of heterochromatin, subtelomeric heterochromatin-adjacent regions, centromeric chromatin, promoters and coding regions. The roles of histone-modification patterns at these domains are discussed.
The fully deacetylated, demethylated state is necessary for repression of gene activity in heterochromatin. Domains that are partially deacetylated might be activated more easily.
Both acetylation and deacetylation are important for gene activity. Certain sites, including H4K16, are hypoacetylated at active genes, and histone deacetylases that deacetylate H4K16 (for example, Hos2) have also been described as activators of transcription.
Hypoacetylation and methylation of certain lysine residues have been shown to affect the binding of chromosomal proteins to target genes. These studies also provide a link between the methylation of a lysine residue (H3K36) and the recruitment of the histone deacetylase Rpd3 to a gene.
Finally, the availability of similar studies in
Schizosaccharomyces pombe
, which is widely divergent in evolution from
S. cerevisiae
, suggests that the findings above might be extrapolated to other eukaryotes.
The recent mapping of histone modifications across the
Saccharomyces cerevisiae
genome has allowed the analysis of how combinations of modified and unmodified chromatin states relate to each other and particularly to chromosomal landmarks, such as heterochromatin, centromeres, promoters and coding regions.
Post-translational histone modifications and histone variants generate complexity in chromatin to enable the many functions of the chromosome. Recent studies have mapped histone modifications across the
Saccharomyces cerevisiae
genome. These experiments describe how combinations of modified and unmodified states relate to each other and particularly to chromosomal landmarks that include heterochromatin, subtelomeric chromatin, centromeres, origins of replication, promoters and coding regions. Such patterns might be important for the regulation of heterochromatin-mediated silencing, chromosome segregation, DNA replication and gene expression.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell cycle</subject><subject>Chromosomes, Fungal - genetics</subject><subject>Chromosomes, Fungal - metabolism</subject><subject>Deoxyribonucleic acid</subject><subject>Developmental Biology</subject><subject>DNA</subject><subject>DNA methylation</subject><subject>DNA Replication - genetics</subject><subject>Enzymes</subject><subject>Gene Expression Regulation, Fungal - genetics</subject><subject>Gene Silencing - physiology</subject><subject>Genome, Fungal - genetics</subject><subject>Genomes</subject><subject>Heterochromatin - genetics</subject><subject>Heterochromatin - metabolism</subject><subject>Histones - genetics</subject><subject>Histones - metabolism</subject><subject>Life Sciences</subject><subject>Protein Processing, Post-Translational - genetics</subject><subject>Proteins</subject><subject>review-article</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Stem Cells</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>1471-0072</issn><issn>1471-0080</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0VtrFDEUB_Agir0ofgJlUPDyMDWXSSZ5LEVroSB4eQ6Z5MyaspNskwzab98ss7asCpKHhJxf_nByEHpG8AnBTL4PaSJKigfokHQ9aTGW-OHduacH6CjnK4yJID1_jA6IUIT2hB8icQ4hTtD-9A6ajSkFUshNHJsfPpcYoJmi86O3pvhYCz40N2ByeYIejWad4eluP0bfP374dvapvfx8fnF2etnaTrHSKkodBukGYaWynWR4HCVzRhFsLDYOc8nZANxySfthUGzAXHWMOYxhkKJjx-j1krtJ8XqGXPTks4X12gSIc9ZC9kISpv4LKRa051hW-PIPeBXnFGoTmtJOCM6IqOjVglZmDdqHMZZk7DZRnxIp6-cRto06-Yeqy8Hkbf280df7vQfv9h5UU-BXWZk5Z33x9cu-fbNYm2LOCUa9SX4y6UYTrLcz17uZV_li19E8TODu3W7IFbxdQK6lsIJ03_LfWc8XGkyZE9xl_a7fAmrXulg</recordid><startdate>20060901</startdate><enddate>20060901</enddate><creator>Millar, Catherine B</creator><creator>Grunstein, Michael</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060901</creationdate><title>Genome-wide patterns of histone modifications in yeast</title><author>Millar, Catherine B ; Grunstein, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c493t-922d0e8db6c89c4830ff83da910ac0ad05853be5c5827bb93b059433d00eb8643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer Research</topic><topic>Cell Biology</topic><topic>Cell cycle</topic><topic>Chromosomes, Fungal - genetics</topic><topic>Chromosomes, Fungal - metabolism</topic><topic>Deoxyribonucleic acid</topic><topic>Developmental Biology</topic><topic>DNA</topic><topic>DNA methylation</topic><topic>DNA Replication - genetics</topic><topic>Enzymes</topic><topic>Gene Expression Regulation, Fungal - genetics</topic><topic>Gene Silencing - physiology</topic><topic>Genome, Fungal - genetics</topic><topic>Genomes</topic><topic>Heterochromatin - genetics</topic><topic>Heterochromatin - metabolism</topic><topic>Histones - genetics</topic><topic>Histones - metabolism</topic><topic>Life Sciences</topic><topic>Protein Processing, Post-Translational - genetics</topic><topic>Proteins</topic><topic>review-article</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Stem Cells</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Millar, Catherine B</creatorcontrib><creatorcontrib>Grunstein, Michael</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>ProQuest Nursing and Allied Health Journals</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database (Proquest)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature reviews. Molecular cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Millar, Catherine B</au><au>Grunstein, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genome-wide patterns of histone modifications in yeast</atitle><jtitle>Nature reviews. Molecular cell biology</jtitle><stitle>Nat Rev Mol Cell Biol</stitle><addtitle>Nat Rev Mol Cell Biol</addtitle><date>2006-09-01</date><risdate>2006</risdate><volume>7</volume><issue>9</issue><spage>657</spage><epage>666</epage><pages>657-666</pages><issn>1471-0072</issn><eissn>1471-0080</eissn><abstract>Key Points
The availability of antibodies that are directed against specific histone-modification sites has allowed the mapping of these sites at the whole-genome level using microarrays. Recent data in
Saccharomyces cerevisiae
are analysed to ask whether unique histone-modification patterns have specific functions.
The preferences of enzymes for particular histone sites and chromosomal locations are described. Different enzymes can affect the same genomic regions to generate unique patterns of modifications.
In particular, there are differences between the histone-modification patterns of heterochromatin, subtelomeric heterochromatin-adjacent regions, centromeric chromatin, promoters and coding regions. The roles of histone-modification patterns at these domains are discussed.
The fully deacetylated, demethylated state is necessary for repression of gene activity in heterochromatin. Domains that are partially deacetylated might be activated more easily.
Both acetylation and deacetylation are important for gene activity. Certain sites, including H4K16, are hypoacetylated at active genes, and histone deacetylases that deacetylate H4K16 (for example, Hos2) have also been described as activators of transcription.
Hypoacetylation and methylation of certain lysine residues have been shown to affect the binding of chromosomal proteins to target genes. These studies also provide a link between the methylation of a lysine residue (H3K36) and the recruitment of the histone deacetylase Rpd3 to a gene.
Finally, the availability of similar studies in
Schizosaccharomyces pombe
, which is widely divergent in evolution from
S. cerevisiae
, suggests that the findings above might be extrapolated to other eukaryotes.
The recent mapping of histone modifications across the
Saccharomyces cerevisiae
genome has allowed the analysis of how combinations of modified and unmodified chromatin states relate to each other and particularly to chromosomal landmarks, such as heterochromatin, centromeres, promoters and coding regions.
Post-translational histone modifications and histone variants generate complexity in chromatin to enable the many functions of the chromosome. Recent studies have mapped histone modifications across the
Saccharomyces cerevisiae
genome. These experiments describe how combinations of modified and unmodified states relate to each other and particularly to chromosomal landmarks that include heterochromatin, subtelomeric chromatin, centromeres, origins of replication, promoters and coding regions. Such patterns might be important for the regulation of heterochromatin-mediated silencing, chromosome segregation, DNA replication and gene expression.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>16912715</pmid><doi>10.1038/nrm1986</doi><tpages>10</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1471-0072 |
ispartof | Nature reviews. Molecular cell biology, 2006-09, Vol.7 (9), p.657-666 |
issn | 1471-0072 1471-0080 |
language | eng |
recordid | cdi_proquest_miscellaneous_68768139 |
source | MEDLINE; SpringerLink_现刊; Nature |
subjects | Biochemistry Biomedical and Life Sciences Cancer Research Cell Biology Cell cycle Chromosomes, Fungal - genetics Chromosomes, Fungal - metabolism Deoxyribonucleic acid Developmental Biology DNA DNA methylation DNA Replication - genetics Enzymes Gene Expression Regulation, Fungal - genetics Gene Silencing - physiology Genome, Fungal - genetics Genomes Heterochromatin - genetics Heterochromatin - metabolism Histones - genetics Histones - metabolism Life Sciences Protein Processing, Post-Translational - genetics Proteins review-article Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Stem Cells Yeast Yeasts |
title | Genome-wide patterns of histone modifications in yeast |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T10%3A13%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Genome-wide%20patterns%20of%20histone%20modifications%20in%20yeast&rft.jtitle=Nature%20reviews.%20Molecular%20cell%20biology&rft.au=Millar,%20Catherine%20B&rft.date=2006-09-01&rft.volume=7&rft.issue=9&rft.spage=657&rft.epage=666&rft.pages=657-666&rft.issn=1471-0072&rft.eissn=1471-0080&rft_id=info:doi/10.1038/nrm1986&rft_dat=%3Cgale_proqu%3EA188912138%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=224665316&rft_id=info:pmid/16912715&rft_galeid=A188912138&rfr_iscdi=true |