A-kinase anchoring protein AKAP95 is implicated in mitotic chromosome condensation by recruiting the condensin complex. Here, we report a differential regulation of condensation of maternal and paternal chromosomes mediated by AKAP95 and chromatin composition in mitotic mouse zygotes. AKAP95 is synthesized upon oocyte activation, targeted to the female pronucleus and specifically associates with maternal chromosomes at mitosis. Peptide competition and rescue experiments show that AKAP95 is required for recruitment of the mCAP-D2 condensin subunit to, and condensation of, maternal chromosomes. In contrast, AKAP95 is dispensable for mCAP-D2 targeting and condensation of paternal chromosomes. In vitro nuclear reconstitution and disassembly assays indicate that human hCAP-D2 targets protamine-containing chromatin independently of AKAP95, but requires AKAP95 for association with histone-containing chromosomes. We propose a concept whereby (1) recruitment of condensins to chromatin is affected by chromatin composition and (2) AKAP95 renders histone-containing chromatin permissive to condensin targeting.
| Identifer | oai:union.ndltd.org:UMASS/oai:scholarworks.umass.edu:dissertations-3658 |
| Date | 01 January 2002 |
| Creators | deRuyter, Jacqueline Leigh |
| Publisher | ScholarWorks@UMass Amherst |
| Source Sets | University of Massachusetts, Amherst |
| Language | English |
| Detected Language | English |
| Type | text |
| Source | Doctoral Dissertations Available from Proquest |
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