Wapl antagonizes cohesin binding and promotes Polycomb-group silencing in Drosophila
| Autor: | Melissa D. Cunningham, Amanda Noyes, Dale Dorsett, James A. Kennison, Judith A. Kassis, Maria Gause, Yuzhong Cheng |
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| Rok vydání: | 2012 |
| Předmět: | |
| Zdroj: | Journal of Cell Science. 125:e1-e1 |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.127126 |
| Popis: | Wapl protein regulates binding of the cohesin complex to chromosomes during interphase and helps remove cohesin from chromosomes at mitosis. We isolated a dominant mutation in wapl (waplAG) in a screen for mutations that counteract silencing mediated by an engrailed Polycomb-group response element. waplAG hemizygotes die as pharate adults and have an extra sex combs phenotype characteristic of males with mutations in Polycomb-group (PcG) genes. The wapl gene encodes two proteins, a long form and a short form. waplAG introduces a stop codon at amino acid 271 of the long form and produces a truncated protein. The expression of a transgene encoding the truncated Wapl-AG protein causes an extra-sex-comb phenotype similar to that seen in the waplAG mutant. Mutations in the cohesin-associated genes Nipped-B and pds5 suppress and enhance waplAG phenotypes, respectively. A Pds5-Wapl complex (releasin) removes cohesin from DNA, while Nipped-B loads cohesin. This suggests that Wapl-AG might exert its effects through changes in cohesin binding. Consistent with this model, Wapl-AG was found to increase the stability of cohesin binding to polytene chromosomes. Our data suggest that increasing cohesin stability interferes with PcG silencing at genes that are co-regulated by cohesin and PcG proteins. |
| Databáze: | OpenAIRE |
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