Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation
The temporal and spatial patterns of histone H3 phosphorylation implicate a specific role for this modification in mammalian chromosome condensation. Cells arrest in late G2 when H3 phosphorylation is competitively inhibited by microinjecting excess substrate at mid-S-phase, suggesting a requirement...
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Veröffentlicht in: | Journal of cell science 1998-12, Vol.111 ( Pt 23) (23), p.3497-3506 |
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container_title | Journal of cell science |
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creator | Van Hooser, A Goodrich, D W Allis, C D Brinkley, B R Mancini, M A |
description | The temporal and spatial patterns of histone H3 phosphorylation implicate a specific role for this modification in mammalian chromosome condensation. Cells arrest in late G2 when H3 phosphorylation is competitively inhibited by microinjecting excess substrate at mid-S-phase, suggesting a requirement for activity of the kinase that phosphorylates H3 during the initiation of chromosome condensation and entry into mitosis. Basal levels of phosphorylated H3 increase primarily in late-replicating/early-condensing heterochromatin both during G2 and when premature chromosome condensation is induced. The prematurely condensed state induced by okadaic acid treatment during S-phase culminates with H3 phosphorylation throughout the chromatin, but in an absence of mitotic chromosome morphology, indicating that the phosphorylation of H3 is not sufficient for complete condensation. Mild hypotonic treatment of cells arrested in mitosis results in the dephosphorylation of H3 without a cytological loss of chromosome compaction. Hypotonic-treated cells, however, complete mitosis only when H3 is phosphorylated. These observations suggest that H3 phosphorylation is required for cell cycle progression and specifically for the changes in chromatin structure incurred during chromosome condensation. |
doi_str_mv | 10.1242/jcs.111.23.3497 |
format | Article |
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Cells arrest in late G2 when H3 phosphorylation is competitively inhibited by microinjecting excess substrate at mid-S-phase, suggesting a requirement for activity of the kinase that phosphorylates H3 during the initiation of chromosome condensation and entry into mitosis. Basal levels of phosphorylated H3 increase primarily in late-replicating/early-condensing heterochromatin both during G2 and when premature chromosome condensation is induced. The prematurely condensed state induced by okadaic acid treatment during S-phase culminates with H3 phosphorylation throughout the chromatin, but in an absence of mitotic chromosome morphology, indicating that the phosphorylation of H3 is not sufficient for complete condensation. Mild hypotonic treatment of cells arrested in mitosis results in the dephosphorylation of H3 without a cytological loss of chromosome compaction. Hypotonic-treated cells, however, complete mitosis only when H3 is phosphorylated. These observations suggest that H3 phosphorylation is required for cell cycle progression and specifically for the changes in chromatin structure incurred during chromosome condensation.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cell Cycle</subject><subject>Cells, Cultured</subject><subject>CHO Cells</subject><subject>Chromosomes - metabolism</subject><subject>Cricetinae</subject><subject>G2 Phase</subject><subject>HeLa Cells</subject><subject>Heterochromatin - metabolism</subject><subject>Histones - genetics</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Hypotonic Solutions</subject><subject>Microscopy, Fluorescence</subject><subject>Mitosis</subject><subject>Molecular Sequence Data</subject><subject>Muntjacs</subject><subject>Phosphorylation</subject><subject>Protamine Kinase - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtLxDAUhYMoOj7WroSsXNnxJmmbZimijiC40XVI0lsm0iZjki7891YdXFwOl_NYfIRcMlgzXvPbD5fXjLE1F2tRK3lAVqyWslJMyEOyAuCsUo0QJ-Q05w8AkFzJY3KsOsaatl6RsvG5xIB0I-huG_Ny6Ws0xcdAfaYJP2efsKdDTLRskfrgi_-1b6idCw2x0Mn4UDCY4PCGxmH5p8mM3gTqtilOMccJqYuhx5B_q-fkaDBjxou9npH3x4e3-0318vr0fH_3UjnBValsN3SgDNqOtS3vAWtRA_bYYuskqL5pLLOL3bSitjA4C24wLTcgFRprmDgj13-7uxQ_Z8xFTz47HEcTMM5ZS4AG6q5Zgrd_QZdizgkHvUt-MulLM9A_nPXCWS-cNRf6h_PSuNpPz3bC_j-_Byu-Af78fFo</recordid><startdate>19981201</startdate><enddate>19981201</enddate><creator>Van Hooser, A</creator><creator>Goodrich, D W</creator><creator>Allis, C D</creator><creator>Brinkley, B R</creator><creator>Mancini, M A</creator><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>7X8</scope></search><sort><creationdate>19981201</creationdate><title>Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation</title><author>Van Hooser, A ; Goodrich, D W ; Allis, C D ; Brinkley, B R ; Mancini, M A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c329t-b8f809aeb81662d0e4340ede6e6c709d55b1baeb5634b0fcb0cfa62a079eaba13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cell Cycle</topic><topic>Cells, Cultured</topic><topic>CHO Cells</topic><topic>Chromosomes - metabolism</topic><topic>Cricetinae</topic><topic>G2 Phase</topic><topic>HeLa Cells</topic><topic>Heterochromatin - metabolism</topic><topic>Histones - genetics</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Hypotonic Solutions</topic><topic>Microscopy, Fluorescence</topic><topic>Mitosis</topic><topic>Molecular Sequence Data</topic><topic>Muntjacs</topic><topic>Phosphorylation</topic><topic>Protamine Kinase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Hooser, A</creatorcontrib><creatorcontrib>Goodrich, D W</creatorcontrib><creatorcontrib>Allis, C D</creatorcontrib><creatorcontrib>Brinkley, B R</creatorcontrib><creatorcontrib>Mancini, M A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Hooser, A</au><au>Goodrich, D W</au><au>Allis, C D</au><au>Brinkley, B R</au><au>Mancini, M A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>1998-12-01</date><risdate>1998</risdate><volume>111 ( Pt 23)</volume><issue>23</issue><spage>3497</spage><epage>3506</epage><pages>3497-3506</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>The temporal and spatial patterns of histone H3 phosphorylation implicate a specific role for this modification in mammalian chromosome condensation. Cells arrest in late G2 when H3 phosphorylation is competitively inhibited by microinjecting excess substrate at mid-S-phase, suggesting a requirement for activity of the kinase that phosphorylates H3 during the initiation of chromosome condensation and entry into mitosis. Basal levels of phosphorylated H3 increase primarily in late-replicating/early-condensing heterochromatin both during G2 and when premature chromosome condensation is induced. The prematurely condensed state induced by okadaic acid treatment during S-phase culminates with H3 phosphorylation throughout the chromatin, but in an absence of mitotic chromosome morphology, indicating that the phosphorylation of H3 is not sufficient for complete condensation. Mild hypotonic treatment of cells arrested in mitosis results in the dephosphorylation of H3 without a cytological loss of chromosome compaction. Hypotonic-treated cells, however, complete mitosis only when H3 is phosphorylated. These observations suggest that H3 phosphorylation is required for cell cycle progression and specifically for the changes in chromatin structure incurred during chromosome condensation.</abstract><cop>England</cop><pmid>9811564</pmid><doi>10.1242/jcs.111.23.3497</doi><tpages>10</tpages></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Company of Biologists |
subjects | Amino Acid Sequence Animals Cell Cycle Cells, Cultured CHO Cells Chromosomes - metabolism Cricetinae G2 Phase HeLa Cells Heterochromatin - metabolism Histones - genetics Histones - metabolism Humans Hypotonic Solutions Microscopy, Fluorescence Mitosis Molecular Sequence Data Muntjacs Phosphorylation Protamine Kinase - metabolism |
title | Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation |
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