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Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation
Treatment of metaphase HTC cells with ZnCl2 inhibits histone phosphatase activity and leads to an increase in the hyperphosphorylated forms of the lysine-rich (F1) histone. Under normal conditions a massive phosphatase activity is triggered as the cells shift from M into G1 phase. In the presence of...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1976
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110976/ https://www.ncbi.nlm.nih.gov/pubmed/1254649 |
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collection | PubMed |
description | Treatment of metaphase HTC cells with ZnCl2 inhibits histone phosphatase activity and leads to an increase in the hyperphosphorylated forms of the lysine-rich (F1) histone. Under normal conditions a massive phosphatase activity is triggered as the cells shift from M into G1 phase. In the presence of ZnCl2 this activity is abolished and thehyperphosphorylated form of F1 persists intact into G1. We have asked the simple question of whether the chromosome can still extend during the M-G1 transition even if the F1 histone is maintained in the hyperphosphorylated form. We observe an apparently normal extension os the chromosomal material under these conditions, though it is evident that high levels of ZnCl2 have rather substantial effects on other cell functions. |
format | Text |
id | pubmed-2110976 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1976 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21109762008-05-01 Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation J Cell Biol Articles Treatment of metaphase HTC cells with ZnCl2 inhibits histone phosphatase activity and leads to an increase in the hyperphosphorylated forms of the lysine-rich (F1) histone. Under normal conditions a massive phosphatase activity is triggered as the cells shift from M into G1 phase. In the presence of ZnCl2 this activity is abolished and thehyperphosphorylated form of F1 persists intact into G1. We have asked the simple question of whether the chromosome can still extend during the M-G1 transition even if the F1 histone is maintained in the hyperphosphorylated form. We observe an apparently normal extension os the chromosomal material under these conditions, though it is evident that high levels of ZnCl2 have rather substantial effects on other cell functions. The Rockefeller University Press 1976-04-01 /pmc/articles/PMC2110976/ /pubmed/1254649 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation |
title | Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation |
title_full | Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation |
title_fullStr | Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation |
title_full_unstemmed | Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation |
title_short | Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation |
title_sort | relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110976/ https://www.ncbi.nlm.nih.gov/pubmed/1254649 |