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Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , |
| In: | Proceedings of the National Academy of Sciences, 103, 2006, 44, S. 16290-16295 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Tang, Xianying Wang, Yanchang Tang, Xianying Wang, Yanchang |
|---|---|
| author |
Tang, Xianying Wang, Yanchang |
| spellingShingle |
Tang, Xianying Wang, Yanchang Proceedings of the National Academy of Sciences Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A Multidisciplinary |
| author_sort |
tang, xianying |
| spelling |
Tang, Xianying Wang, Yanchang 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0607856103 <jats:p> Spindle disruption or DNA damage prevents sister chromatid separation through the activation of checkpoint pathways that inhibit anaphase entry by stabilizing the anaphase inhibitor Pds1. Mutation of <jats:italic>CDC55</jats:italic> , which encodes a B regulatory subunit of protein phosphatase 2A (PP2A), results in precocious sister chromatid separation when spindle is disrupted. Here we report that decreased Pds1 levels in <jats:italic>Δcdc55</jats:italic> mutants contribute to sister chromatid separation in the presence of nocodazole, a microtubule-depolymerizing drug. However, in the presence of DNA damage, <jats:italic>Δcdc55</jats:italic> mutant cells separate sister chromatids without noticeable decrease of Pds1 or cohesin Mcd1/Scc1 levels. Further analysis demonstrates that <jats:italic>Δcdc55</jats:italic> mutants lose cohesion along the entire chromosomes when the spindle is disrupted. In contrast, separation of sister chromatids is limited to the centromeric regions in <jats:italic>Δcdc55</jats:italic> cells after DNA damage. Moreover, mutation of <jats:italic>TPD3</jats:italic> , which encodes the A regulatory subunit of PP2A, also results in sister chromatid separation in DNA- or spindle-damage-arrested cells. These data suggest that PP2A regulates sister chromatid cohesion in Pds1-dependent and -independent manners. </jats:p> Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A Proceedings of the National Academy of Sciences |
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Proceedings of the National Academy of Sciences, 2006 |
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Proceedings of the National Academy of Sciences, 2006 |
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| title |
Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_unstemmed |
Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_full |
Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_fullStr |
Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_full_unstemmed |
Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_short |
Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_sort |
pds1/esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2a |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.0607856103 |
| publishDate |
2006 |
| physical |
16290-16295 |
| description |
<jats:p>
Spindle disruption or DNA damage prevents sister chromatid separation through the activation of checkpoint pathways that inhibit anaphase entry by stabilizing the anaphase inhibitor Pds1. Mutation of
<jats:italic>CDC55</jats:italic>
, which encodes a B regulatory subunit of protein phosphatase 2A (PP2A), results in precocious sister chromatid separation when spindle is disrupted. Here we report that decreased Pds1 levels in
<jats:italic>Δcdc55</jats:italic>
mutants contribute to sister chromatid separation in the presence of nocodazole, a microtubule-depolymerizing drug. However, in the presence of DNA damage,
<jats:italic>Δcdc55</jats:italic>
mutant cells separate sister chromatids without noticeable decrease of Pds1 or cohesin Mcd1/Scc1 levels. Further analysis demonstrates that
<jats:italic>Δcdc55</jats:italic>
mutants lose cohesion along the entire chromosomes when the spindle is disrupted. In contrast, separation of sister chromatids is limited to the centromeric regions in
<jats:italic>Δcdc55</jats:italic>
cells after DNA damage. Moreover, mutation of
<jats:italic>TPD3</jats:italic>
, which encodes the A regulatory subunit of PP2A, also results in sister chromatid separation in DNA- or spindle-damage-arrested cells. These data suggest that PP2A regulates sister chromatid cohesion in Pds1-dependent and -independent manners.
</jats:p> |
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| author | Tang, Xianying, Wang, Yanchang |
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| container_title | Proceedings of the National Academy of Sciences |
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| description | <jats:p> Spindle disruption or DNA damage prevents sister chromatid separation through the activation of checkpoint pathways that inhibit anaphase entry by stabilizing the anaphase inhibitor Pds1. Mutation of <jats:italic>CDC55</jats:italic> , which encodes a B regulatory subunit of protein phosphatase 2A (PP2A), results in precocious sister chromatid separation when spindle is disrupted. Here we report that decreased Pds1 levels in <jats:italic>Δcdc55</jats:italic> mutants contribute to sister chromatid separation in the presence of nocodazole, a microtubule-depolymerizing drug. However, in the presence of DNA damage, <jats:italic>Δcdc55</jats:italic> mutant cells separate sister chromatids without noticeable decrease of Pds1 or cohesin Mcd1/Scc1 levels. Further analysis demonstrates that <jats:italic>Δcdc55</jats:italic> mutants lose cohesion along the entire chromosomes when the spindle is disrupted. In contrast, separation of sister chromatids is limited to the centromeric regions in <jats:italic>Δcdc55</jats:italic> cells after DNA damage. Moreover, mutation of <jats:italic>TPD3</jats:italic> , which encodes the A regulatory subunit of PP2A, also results in sister chromatid separation in DNA- or spindle-damage-arrested cells. These data suggest that PP2A regulates sister chromatid cohesion in Pds1-dependent and -independent manners. </jats:p> |
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| spelling | Tang, Xianying Wang, Yanchang 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0607856103 <jats:p> Spindle disruption or DNA damage prevents sister chromatid separation through the activation of checkpoint pathways that inhibit anaphase entry by stabilizing the anaphase inhibitor Pds1. Mutation of <jats:italic>CDC55</jats:italic> , which encodes a B regulatory subunit of protein phosphatase 2A (PP2A), results in precocious sister chromatid separation when spindle is disrupted. Here we report that decreased Pds1 levels in <jats:italic>Δcdc55</jats:italic> mutants contribute to sister chromatid separation in the presence of nocodazole, a microtubule-depolymerizing drug. However, in the presence of DNA damage, <jats:italic>Δcdc55</jats:italic> mutant cells separate sister chromatids without noticeable decrease of Pds1 or cohesin Mcd1/Scc1 levels. Further analysis demonstrates that <jats:italic>Δcdc55</jats:italic> mutants lose cohesion along the entire chromosomes when the spindle is disrupted. In contrast, separation of sister chromatids is limited to the centromeric regions in <jats:italic>Δcdc55</jats:italic> cells after DNA damage. Moreover, mutation of <jats:italic>TPD3</jats:italic> , which encodes the A regulatory subunit of PP2A, also results in sister chromatid separation in DNA- or spindle-damage-arrested cells. These data suggest that PP2A regulates sister chromatid cohesion in Pds1-dependent and -independent manners. </jats:p> Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A Proceedings of the National Academy of Sciences |
| spellingShingle | Tang, Xianying, Wang, Yanchang, Proceedings of the National Academy of Sciences, Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A, Multidisciplinary |
| title | Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_full | Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_fullStr | Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_full_unstemmed | Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_short | Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| title_sort | pds1/esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2a |
| title_unstemmed | Pds1/Esp1-dependent and -independent sister chromatid separation in mutants defective for protein phosphatase 2A |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.0607856103 |